Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings

This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric po...

Full description

Saved in:
Bibliographic Details
Published in3 Biotech Vol. 6; no. 1; pp. 113 - 8
Main Authors Aanangi, Raveendra, Kotapati, Kasi Viswanath, Palaka, Bhagath Kumar, Kedam, Thyagaraju, Kanika, Nirmala Devi, Ampasala, Dinakara Rao
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer Berlin Heidelberg 01.06.2016
Springer Nature B.V
Subjects
Online AccessGet full text
ISSN2190-572X
2190-5738
DOI10.1007/s13205-016-0427-5

Cover

Loading…
Abstract This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
AbstractList This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 degree C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant alpha -helix and beta -strands. Further, the secondary structure of mung bean LOX was stable up to 60 degree C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant [alpha]-helix and [beta]-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX.
ArticleNumber 113
Author Kedam, Thyagaraju
Aanangi, Raveendra
Ampasala, Dinakara Rao
Palaka, Bhagath Kumar
Kotapati, Kasi Viswanath
Kanika, Nirmala Devi
Author_xml – sequence: 1
  givenname: Raveendra
  surname: Aanangi
  fullname: Aanangi, Raveendra
  organization: Department of Biochemistry, Sri Venkateswara University
– sequence: 2
  givenname: Kasi Viswanath
  surname: Kotapati
  fullname: Kotapati, Kasi Viswanath
  organization: Centre for Bioinformatics, School of Life sciences, Pondicherry University
– sequence: 3
  givenname: Bhagath Kumar
  surname: Palaka
  fullname: Palaka, Bhagath Kumar
  organization: Centre for Bioinformatics, School of Life sciences, Pondicherry University
– sequence: 4
  givenname: Thyagaraju
  surname: Kedam
  fullname: Kedam, Thyagaraju
  organization: Department of Biochemistry, Sri Venkateswara University
– sequence: 5
  givenname: Nirmala Devi
  surname: Kanika
  fullname: Kanika, Nirmala Devi
  organization: Department of Biochemistry, Sri Venkateswara University
– sequence: 6
  givenname: Dinakara Rao
  surname: Ampasala
  fullname: Ampasala, Dinakara Rao
  email: ampasaladr@bicpu.edu.in
  organization: Centre for Bioinformatics, School of Life sciences, Pondicherry University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28330183$$D View this record in MEDLINE/PubMed
BookMark eNqNkk1vFiEUhYmpsfW1P8CNmcRNXUzlwjAwGxPT-JW8iS7UuCO3DExpZuAVZoz110udtqlN_GABBJ5zwuWeh2QvxGAJeQz0GCiVzzNwRkVNoa1pw2Qt7pEDBh2theRq72bPvuyTw5zPaRkCRAf0AdlninMKih8Q_2FJ3nmDs4-hwtBX5gwTmtkm_2M9jK4a_S5-vxhswGwrl-JUTUsYqlOLoTr67IeAVcLe44zV9vhZNdg0-VDUhcnW9mPZ5EfkvsMx28OrdUM-vX718eRtvX3_5t3Jy21tBG_nmnfgwCKjvIVegmMWgUrXCsYQTGec6dFZ2THTGMfBOFHmpunLqZGsk3xDXqy-u-V0sr2xYU446l3yE6YLHdHr32-CP9ND_KYF7xR0vBgcXRmk-HWxedaTz8aOIwYbl6wZZVS1XDH5TxSUok0rmWL_gRbT0heqCvr0DnoelxTKpxUKOBVNy5tCPbld502B170tgFwBk2LOyTpt_PyrpaVsP2qg-jJIeg2SLkHSl0Eq_7AhcEd5bf43DVs1ubChJODWo_8o-gncSNpb
CitedBy_id crossref_primary_10_12944_CRNFSJ_9_3_09
crossref_primary_10_4025_actasciagron_v44i1_53434
crossref_primary_10_33003_fjs_2023_0703_1843
crossref_primary_10_3390_foods12132504
crossref_primary_10_1021_acsfoodscitech_3c00242
crossref_primary_10_1002_leg3_44
crossref_primary_10_3390_plants11070979
crossref_primary_10_3389_fpls_2022_1069143
crossref_primary_10_1007_s00253_024_13335_8
crossref_primary_10_3389_fmicb_2024_1363256
crossref_primary_10_1039_D1EN00845E
crossref_primary_10_1016_j_foodchem_2020_127583
crossref_primary_10_1016_j_bcab_2023_102838
crossref_primary_10_1002_slct_202203961
Cites_doi 10.1074/jbc.274.34.23679
10.1016/0003-2697(90)90525-E
10.1002/jsfa.2740240906
10.1016/0076-6879(81)71055-3
10.1146/annurev.pp.42.060191.001045
10.1002/jsfa.3958
10.1016/j.biotechadv.2012.04.004
10.1007/s40502-015-0186-z
10.1021/jf980853z
10.1021/jf990463s
10.1271/bbb.61.347
10.1105/tpc.13.3.613
10.1104/pp.114.251298
10.1021/jf060022q
10.1016/0076-6879(90)87031-W
10.1042/BJ20051889
10.1146/annurev.arplant.53.100301.135248
10.1080/1475636021000006243
10.1093/jxb/err030
10.1016/S0014-5793(99)00396-8
10.1002/biot.200700097
10.1096/fj.09-141390
10.1016/S0308-8146(98)00042-9
10.1016/0005-2744(70)90123-3
10.1038/227680a0
10.3109/14756369809036547
10.1016/S1360-1385(01)01950-1
10.1016/0014-5793(91)80227-T
ContentType Journal Article
Copyright The Author(s) 2016
King Abdulaziz City for Science and Technology 2016
Copyright_xml – notice: The Author(s) 2016
– notice: King Abdulaziz City for Science and Technology 2016
DBID C6C
AAYXX
CITATION
NPM
8AO
8FE
8FG
8FH
ABJCF
AFKRA
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
CCPQU
DWQXO
GNUQQ
HCIFZ
L6V
LK8
M7P
M7S
PHGZM
PHGZT
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
PTHSS
7QO
8FD
FR3
P64
7X8
7S9
L.6
5PM
DOI 10.1007/s13205-016-0427-5
DatabaseName Springer Nature OA Free Journals
CrossRef
PubMed
ProQuest Pharma Collection
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Materials Science & Engineering Collection
ProQuest Central UK/Ireland
ProQuest Central Essentials - QC
Biological Science Collection
ProQuest Central
Technology Collection
Natural Science Collection
ProQuest One
ProQuest Central Korea
ProQuest Central Student
SciTech Premium Collection
ProQuest Engineering Collection
ProQuest Biological Science Collection
Biological Science Database
Engineering Database
ProQuest Central Premium
ProQuest One Academic (New)
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Engineering Collection
Biotechnology Research Abstracts
Technology Research Database
Engineering Research Database
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
PubMed
ProQuest Central Student
Technology Collection
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
ProQuest Engineering Collection
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Central (New)
Engineering Collection
Engineering Database
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
ProQuest Technology Collection
Biological Science Database
ProQuest SciTech Collection
ProQuest One Academic UKI Edition
Materials Science & Engineering Collection
ProQuest One Academic
ProQuest One Academic (New)
Engineering Research Database
Biotechnology Research Abstracts
Technology Research Database
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList AGRICOLA
Engineering Research Database

ProQuest Central Student
MEDLINE - Academic

PubMed
Database_xml – sequence: 1
  dbid: C6C
  name: Springer Nature OA Free Journals
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 3
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Economics
Chemistry
Agriculture
EISSN 2190-5738
EndPage 8
ExternalDocumentID PMC5398193
4155336021
28330183
10_1007_s13205_016_0427_5
Genre Journal Article
GeographicLocations India
GeographicLocations_xml – name: India
GrantInformation_xml – fundername: Department of Biotechnology , Ministry of Science and Technology
  grantid: No: BT/PR10858/AGR/02/682/2008
  funderid: http://dx.doi.org/10.13039/501100001407
– fundername: ;
  grantid: No: BT/PR10858/AGR/02/682/2008
GroupedDBID -A0
-EM
0R~
2VQ
4.4
406
40G
53G
8AO
8FE
8FG
8FH
AAAVM
AACDK
AAHBH
AAHNG
AAJBT
AANZL
AASML
AATNV
AATVU
AAUYE
ABAKF
ABDBF
ABDZT
ABECU
ABFTV
ABJCF
ABJNI
ABJOX
ABKCH
ABMQK
ABSXP
ABTEG
ABTKH
ABTMW
ABXPI
ACAOD
ACDTI
ACGFS
ACHSB
ACIWK
ACMLO
ACOKC
ACPIV
ACPRK
ACUHS
ACZOJ
ADBBV
ADDVE
ADHHG
ADINQ
ADKNI
ADKPE
ADRAZ
ADTPH
ADURQ
ADYFF
ADZKW
AEFQL
AEGXH
AEJRE
AEMSY
AENEX
AEOHA
AEPYU
AESKC
AEVLU
AEXYK
AFBBN
AFKRA
AFQWF
AGDGC
AGJBK
AGMZJ
AGQEE
AGRTI
AHBYD
AHSBF
AHYZX
AIAKS
AIGIU
AILAN
AITGF
AJRNO
AJZVZ
ALMA_UNASSIGNED_HOLDINGS
AMKLP
AMTXH
AMXSW
AMYLF
AMYQR
AOIJS
AXYYD
BBNVY
BENPR
BGLVJ
BGNMA
BHPHI
C24
C6C
CCPQU
CSCUP
DNIVK
DPUIP
EBLON
EBS
EIOEI
EJD
FERAY
FFXSO
FIGPU
FINBP
FNLPD
FSGXE
GGCAI
GJIRD
GX1
H4N
HCIFZ
HYE
HZ~
IKXTQ
IWAJR
J-C
JZLTJ
KOV
KQ8
L6V
LK8
LLZTM
M48
M4Y
M7P
M7S
M~E
NPVJJ
NQJWS
NU0
O9-
O9J
OK1
PT4
PTHSS
RNS
ROL
RPM
RSV
SCM
SISQX
SJYHP
SNE
SNPRN
SNX
SOHCF
SOJ
SPISZ
SRMVM
SSLCW
STPWE
TSG
U2A
UOJIU
UTJUX
UZXMN
VFIZW
Z5O
Z7U
Z7V
Z7W
Z7Y
Z83
ZMTXR
AAYXX
ABBRH
ABDBE
ABFSG
ACMFV
ACSTC
AEZWR
AFDZB
AFHIU
AFOHR
AHPBZ
AHWEU
AIXLP
ATHPR
AYFIA
CITATION
PHGZM
PHGZT
ABRTQ
NPM
PQGLB
AZQEC
DWQXO
GNUQQ
PKEHL
PQEST
PQQKQ
PQUKI
PRINS
7QO
8FD
FR3
P64
PUEGO
7X8
7S9
L.6
5PM
ID FETCH-LOGICAL-c536t-391f1ea20361d71f2ea107f6522a1c9cfcdafe792c4cf31cf5f3144ddafc72973
IEDL.DBID M48
ISSN 2190-572X
IngestDate Thu Aug 21 18:04:20 EDT 2025
Thu Sep 04 19:09:31 EDT 2025
Fri Sep 05 10:27:20 EDT 2025
Fri Sep 05 10:14:11 EDT 2025
Fri Jul 25 11:18:55 EDT 2025
Mon Jul 21 06:04:27 EDT 2025
Thu Apr 24 23:08:45 EDT 2025
Tue Jul 01 04:21:25 EDT 2025
Fri Feb 21 02:26:20 EST 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Keywords Plant lipoxygenases
Protein purification
Chromatofocusing
Circular dichroism
Mung bean
Language English
License Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c536t-391f1ea20361d71f2ea107f6522a1c9cfcdafe792c4cf31cf5f3144ddafc72973
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
OpenAccessLink http://journals.scholarsportal.info/openUrl.xqy?doi=10.1007/s13205-016-0427-5
PMID 28330183
PQID 1813054634
PQPubID 2034528
PageCount 8
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5398193
proquest_miscellaneous_2020863827
proquest_miscellaneous_1880467282
proquest_miscellaneous_1808628308
proquest_journals_1813054634
pubmed_primary_28330183
crossref_citationtrail_10_1007_s13205_016_0427_5
crossref_primary_10_1007_s13205_016_0427_5
springer_journals_10_1007_s13205_016_0427_5
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 20160600
PublicationDateYYYYMMDD 2016-06-01
PublicationDate_xml – month: 6
  year: 2016
  text: 20160600
PublicationDecade 2010
PublicationPlace Berlin/Heidelberg
PublicationPlace_xml – name: Berlin/Heidelberg
– name: Germany
– name: Heidelberg
PublicationTitle 3 Biotech
PublicationTitleAbbrev 3 Biotech
PublicationTitleAlternate 3 Biotech
PublicationYear 2016
Publisher Springer Berlin Heidelberg
Springer Nature B.V
Publisher_xml – name: Springer Berlin Heidelberg
– name: Springer Nature B.V
References Devi, Lakshmi, Reddy, Reddanna (CR7) 2005; 28
Barone (CR2) 1999; 47
Dainese, Angelucci, Sabatucci, De Filippis, Mei, Maccarrone (CR6) 2010; 24
Kotapati, Bhagath Kumar, Raveendra, Thyagarju, Dinakara rao (CR16) 2015; 20
Clemente, Olías, Olías (CR5) 2000; 48
Suzuki (CR29) 2010; 90
Rao, Devi, Thyagaraju (CR24) 1998; 14
Joo, Oh (CR15) 2012; 30
Gfeller, Liechti, Farmer (CR11) 2010; 3
Reddanna, Whelan, Maddipati, Reddy (CR25) 1990; 187
Kuhn, Thiele (CR20) 1999; 449
Heydeck, Schewe (CR14) 1984; 44
Haydar, Hadziyev (CR13) 1973; 24
Rehbock, Ganßer, Berger (CR26) 1998; 63
van Aarle, de Barse, Veldink, Vliegenthart (CR30) 1991; 280
Graff, Anderson, Jaques (CR12) 1990; 188
Chow (CR4) 2007; 2
Eriksson, Svensson (CR8) 1970; 198
Feussner, Kuhn, Wasternack (CR10) 2001; 6
Kohyama, Nagata, SI, Sekiya (CR17) 1997; 61
Kuo, Hwang, Yeh, Pan, Tsai, Pan (CR21) 2006; 54
Nagabhushana, Umamaheshwari, Tocoli, Prabhu, Green, Ramadoss (CR23) 2002; 17
Siedow (CR28) 1991; 42
Kolomiets, Hannapel, Chen, Tymeson, Gladon (CR18) 2001; 13
Brash (CR3) 1999; 274
Laemmli (CR22) 1970; 227
Feussner, Wasternack (CR9) 2002; 53
Kong, Ju, Parihar, Kim, Cho, Kwak (CR19) 2015; 167
Roopashree, Singh, Gowda, Rao (CR27) 2006; 395
Weitbrecht, Muller, Leubner-Metzger (CR31) 2011; 62
Axelrod, Cheesbrough, Laakso (CR1) 1981; 71
H Kuhn (427_CR20) 1999; 449
A Clemente (427_CR5) 2000; 48
P Devi (427_CR7) 2005; 28
UK Laemmli (427_CR22) 1970; 227
PG Aarle van (427_CR30) 1991; 280
N Kohyama (427_CR17) 1997; 61
M Haydar (427_CR13) 1973; 24
D Heydeck (427_CR14) 1984; 44
YC Joo (427_CR15) 2012; 30
T Suzuki (427_CR29) 2010; 90
S Roopashree (427_CR27) 2006; 395
JN Siedow (427_CR28) 1991; 42
KS Nagabhushana (427_CR23) 2002; 17
R Barone (427_CR2) 1999; 47
I Feussner (427_CR10) 2001; 6
K Weitbrecht (427_CR31) 2011; 62
A Gfeller (427_CR11) 2010; 3
B Axelrod (427_CR1) 1981; 71
Y Chow (427_CR4) 2007; 2
D Kong (427_CR19) 2015; 167
JM Kuo (427_CR21) 2006; 54
C Eriksson (427_CR8) 1970; 198
E Dainese (427_CR6) 2010; 24
G Graff (427_CR12) 1990; 188
P Reddanna (427_CR25) 1990; 187
MV Kolomiets (427_CR18) 2001; 13
A Rao (427_CR24) 1998; 14
KV Kotapati (427_CR16) 2015; 20
I Feussner (427_CR9) 2002; 53
AR Brash (427_CR3) 1999; 274
B Rehbock (427_CR26) 1998; 63
References_xml – volume: 28
  start-page: 87
  year: 2005
  end-page: 93
  ident: CR7
  article-title: Differential expression of upoxygenase in green gram ( L.)
  publication-title: Legum Res Int J
– volume: 274
  start-page: 23679
  year: 1999
  end-page: 23682
  ident: CR3
  article-title: Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate
  publication-title: J Biol Chem
  doi: 10.1074/jbc.274.34.23679
– volume: 188
  start-page: 38
  year: 1990
  end-page: 47
  ident: CR12
  article-title: Preparation and purification of soybean lipoxygenase-derived unsaturated hydroperoxy and hydroxy fatty acids and determination of molar absorptivities of hydroxy fatty acids
  publication-title: Anal Biochem
  doi: 10.1016/0003-2697(90)90525-E
– volume: 24
  start-page: 1039
  year: 1973
  end-page: 1053
  ident: CR13
  article-title: A study of lipoxidase in pea seeds and seedlings
  publication-title: J Sci Food Agric
  doi: 10.1002/jsfa.2740240906
– volume: 71
  start-page: 441
  year: 1981
  end-page: 451
  ident: CR1
  article-title: Lipoxygenase from soybeans
  publication-title: Methods Enzymol
  doi: 10.1016/0076-6879(81)71055-3
– volume: 42
  start-page: 145
  year: 1991
  end-page: 188
  ident: CR28
  article-title: Plant lipoxygenase: structure and function
  publication-title: Ann Rev Plant Biol
  doi: 10.1146/annurev.pp.42.060191.001045
– volume: 90
  start-page: 1232
  year: 2010
  end-page: 1237
  ident: CR29
  article-title: Effects of lipase, lipoxygenase, peroxidase and free fatty acids on volatile compound found in boiled buckwheat noodles
  publication-title: J Sci Food Agric
  doi: 10.1002/jsfa.3958
– volume: 30
  start-page: 1524
  year: 2012
  end-page: 1532
  ident: CR15
  article-title: Lipoxygenases: potential starting biocatalysts for the synthesis of signaling compounds
  publication-title: Biotechnol Adv
  doi: 10.1016/j.biotechadv.2012.04.004
– volume: 20
  start-page: 345
  year: 2015
  end-page: 352
  ident: CR16
  article-title: Cloning and characterization of lipoxygenase gene from germinating seedlings of green gram ( L.)
  publication-title: Indian J Plant Physiol
  doi: 10.1007/s40502-015-0186-z
– volume: 47
  start-page: 1924
  year: 1999
  end-page: 1931
  ident: CR2
  article-title: Purification and characterization of a lipoxygenase enzyme from durum wheat semolina
  publication-title: J Agric Food Chem
  doi: 10.1021/jf980853z
– volume: 3
  start-page: 109
  year: 2010
  ident: CR11
  article-title: Arabidopsis jasmonate signaling pathway
  publication-title: Sci Signal
– volume: 48
  start-page: 1070
  year: 2000
  end-page: 1075
  ident: CR5
  article-title: Purification and characterization of broad bean lipoxygenase isoenzymes
  publication-title: J Agric Food Chem
  doi: 10.1021/jf990463s
– volume: 61
  start-page: 347
  year: 1997
  end-page: 350
  ident: CR17
  article-title: Inhibition of arachidonate lipoxygenase activities by 2-(3, 4-dihydroxyphenyl) ethanol, a phenolic compound from olives
  publication-title: Biosci Biotechnol Biochem
  doi: 10.1271/bbb.61.347
– volume: 13
  start-page: 613
  year: 2001
  end-page: 626
  ident: CR18
  article-title: Lipoxygenase is involved in the control of potato tuber development
  publication-title: Plant Cell
  doi: 10.1105/tpc.13.3.613
– volume: 167
  start-page: 1630
  year: 2015
  end-page: 1642
  ident: CR19
  article-title: Arabidopsis glutamate receptor homolog AtGLR3.5 modulates cytosolic Ca  level to counteract effect of abscisic acid in seed germination
  publication-title: Plant Physiol
  doi: 10.1104/pp.114.251298
– volume: 54
  start-page: 3151
  year: 2006
  end-page: 3156
  ident: CR21
  article-title: Lipoxygenase from banana leaf: purification and characterization of an enzyme that catalyzes linoleic acid oxygenation at the 9-position
  publication-title: J Agric Food Chem
  doi: 10.1021/jf060022q
– volume: 187
  start-page: 268
  year: 1990
  end-page: 277
  ident: CR25
  article-title: Purification of arachidonate 5-lipoxygenase from potato tubers
  publication-title: Methods Enzymol
  doi: 10.1016/0076-6879(90)87031-W
– volume: 395
  start-page: 629
  year: 2006
  end-page: 639
  ident: CR27
  article-title: Dual-function protein in plant defence: seed lectin from Dolichos biflorus (horse gram) exhibits lipoxygenase activity
  publication-title: Biochem J
  doi: 10.1042/BJ20051889
– volume: 53
  start-page: 275
  year: 2002
  end-page: 297
  ident: CR9
  article-title: The lipoxygenase pathway
  publication-title: Ann Rev Plant Biol
  doi: 10.1146/annurev.arplant.53.100301.135248
– volume: 17
  start-page: 255
  year: 2002
  end-page: 259
  ident: CR23
  article-title: Inhibition of soybean and potato Lipoxygenases by Bhilawanols from Bhilawan ( ) nut shell liquid and some synthetic Salicylic acid analogues
  publication-title: J Enzyme Inhib Med Chem
  doi: 10.1080/1475636021000006243
– volume: 62
  start-page: 3289
  issue: 10
  year: 2011
  end-page: 3309
  ident: CR31
  article-title: First off the mark: early seed germination
  publication-title: J Exp Bot
  doi: 10.1093/jxb/err030
– volume: 449
  start-page: 7
  year: 1999
  end-page: 11
  ident: CR20
  article-title: The diversity of the lipoxygenase family
  publication-title: FEBS Lett
  doi: 10.1016/S0014-5793(99)00396-8
– volume: 2
  start-page: 1375
  year: 2007
  end-page: 1380
  ident: CR4
  article-title: Mung bean lipoxygenase in the production of a C6-aldehyde. Natural green-note flavor generation via biotransformation
  publication-title: Biotechnol J
  doi: 10.1002/biot.200700097
– volume: 24
  start-page: 1725
  year: 2010
  end-page: 1736
  ident: CR6
  article-title: A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1
  publication-title: FASEB J
  doi: 10.1096/fj.09-141390
– volume: 63
  start-page: 161
  year: 1998
  end-page: 165
  ident: CR26
  article-title: Efficient generation of 2E-hexenal by a hydroperoxide lyase from mung bean seedlings
  publication-title: Food Chem
  doi: 10.1016/S0308-8146(98)00042-9
– volume: 44
  start-page: 1261
  year: 1984
  end-page: 1263
  ident: CR14
  article-title: Improved procedure for the detection of activity of lipoxygenases on electropherograms
  publication-title: Biomed Biochim Acta
– volume: 198
  start-page: 449
  year: 1970
  end-page: 459
  ident: CR8
  article-title: Lipoxygenase from peas, purification and properties of the enzyme
  publication-title: Biochimica et Biophysica Acta (BBA) Enzymol
  doi: 10.1016/0005-2744(70)90123-3
– volume: 227
  start-page: 680
  year: 1970
  end-page: 685
  ident: CR22
  article-title: Cleavage of structural proteins during the assembly of the head of bacteriophage T4
  publication-title: Nature
  doi: 10.1038/227680a0
– volume: 14
  start-page: 85
  year: 1998
  end-page: 96
  ident: CR24
  article-title: Isolation of antioxidant principle from azadzrachta seed kernels: determination of its role on plant lipoxygenases
  publication-title: J Enzym Inhib
  doi: 10.3109/14756369809036547
– volume: 6
  start-page: 268
  issue: 6
  year: 2001
  end-page: 273
  ident: CR10
  article-title: Lipoxygenase-dependent degradation of storage lipids
  publication-title: Trends Plant Sci
  doi: 10.1016/S1360-1385(01)01950-1
– volume: 280
  start-page: 159
  year: 1991
  end-page: 162
  ident: CR30
  article-title: Purification of a lipoxygenase from ungerminated barley Characterization and product formation
  publication-title: FEBS Lett
  doi: 10.1016/0014-5793(91)80227-T
– volume: 54
  start-page: 3151
  year: 2006
  ident: 427_CR21
  publication-title: J Agric Food Chem
  doi: 10.1021/jf060022q
– volume: 44
  start-page: 1261
  year: 1984
  ident: 427_CR14
  publication-title: Biomed Biochim Acta
– volume: 188
  start-page: 38
  year: 1990
  ident: 427_CR12
  publication-title: Anal Biochem
  doi: 10.1016/0003-2697(90)90525-E
– volume: 28
  start-page: 87
  year: 2005
  ident: 427_CR7
  publication-title: Legum Res Int J
– volume: 24
  start-page: 1725
  year: 2010
  ident: 427_CR6
  publication-title: FASEB J
  doi: 10.1096/fj.09-141390
– volume: 20
  start-page: 345
  year: 2015
  ident: 427_CR16
  publication-title: Indian J Plant Physiol
  doi: 10.1007/s40502-015-0186-z
– volume: 449
  start-page: 7
  year: 1999
  ident: 427_CR20
  publication-title: FEBS Lett
  doi: 10.1016/S0014-5793(99)00396-8
– volume: 2
  start-page: 1375
  year: 2007
  ident: 427_CR4
  publication-title: Biotechnol J
  doi: 10.1002/biot.200700097
– volume: 280
  start-page: 159
  year: 1991
  ident: 427_CR30
  publication-title: FEBS Lett
  doi: 10.1016/0014-5793(91)80227-T
– volume: 198
  start-page: 449
  year: 1970
  ident: 427_CR8
  publication-title: Biochimica et Biophysica Acta (BBA) Enzymol
  doi: 10.1016/0005-2744(70)90123-3
– volume: 187
  start-page: 268
  year: 1990
  ident: 427_CR25
  publication-title: Methods Enzymol
  doi: 10.1016/0076-6879(90)87031-W
– volume: 61
  start-page: 347
  year: 1997
  ident: 427_CR17
  publication-title: Biosci Biotechnol Biochem
  doi: 10.1271/bbb.61.347
– volume: 24
  start-page: 1039
  year: 1973
  ident: 427_CR13
  publication-title: J Sci Food Agric
  doi: 10.1002/jsfa.2740240906
– volume: 17
  start-page: 255
  year: 2002
  ident: 427_CR23
  publication-title: J Enzyme Inhib Med Chem
  doi: 10.1080/1475636021000006243
– volume: 227
  start-page: 680
  year: 1970
  ident: 427_CR22
  publication-title: Nature
  doi: 10.1038/227680a0
– volume: 62
  start-page: 3289
  issue: 10
  year: 2011
  ident: 427_CR31
  publication-title: J Exp Bot
  doi: 10.1093/jxb/err030
– volume: 53
  start-page: 275
  year: 2002
  ident: 427_CR9
  publication-title: Ann Rev Plant Biol
  doi: 10.1146/annurev.arplant.53.100301.135248
– volume: 30
  start-page: 1524
  year: 2012
  ident: 427_CR15
  publication-title: Biotechnol Adv
  doi: 10.1016/j.biotechadv.2012.04.004
– volume: 42
  start-page: 145
  year: 1991
  ident: 427_CR28
  publication-title: Ann Rev Plant Biol
  doi: 10.1146/annurev.pp.42.060191.001045
– volume: 47
  start-page: 1924
  year: 1999
  ident: 427_CR2
  publication-title: J Agric Food Chem
  doi: 10.1021/jf980853z
– volume: 274
  start-page: 23679
  year: 1999
  ident: 427_CR3
  publication-title: J Biol Chem
  doi: 10.1074/jbc.274.34.23679
– volume: 6
  start-page: 268
  issue: 6
  year: 2001
  ident: 427_CR10
  publication-title: Trends Plant Sci
  doi: 10.1016/S1360-1385(01)01950-1
– volume: 3
  start-page: 109
  year: 2010
  ident: 427_CR11
  publication-title: Sci Signal
– volume: 63
  start-page: 161
  year: 1998
  ident: 427_CR26
  publication-title: Food Chem
  doi: 10.1016/S0308-8146(98)00042-9
– volume: 48
  start-page: 1070
  year: 2000
  ident: 427_CR5
  publication-title: J Agric Food Chem
  doi: 10.1021/jf990463s
– volume: 71
  start-page: 441
  year: 1981
  ident: 427_CR1
  publication-title: Methods Enzymol
  doi: 10.1016/0076-6879(81)71055-3
– volume: 13
  start-page: 613
  year: 2001
  ident: 427_CR18
  publication-title: Plant Cell
  doi: 10.1105/tpc.13.3.613
– volume: 395
  start-page: 629
  year: 2006
  ident: 427_CR27
  publication-title: Biochem J
  doi: 10.1042/BJ20051889
– volume: 167
  start-page: 1630
  year: 2015
  ident: 427_CR19
  publication-title: Plant Physiol
  doi: 10.1104/pp.114.251298
– volume: 14
  start-page: 85
  year: 1998
  ident: 427_CR24
  publication-title: J Enzym Inhib
  doi: 10.3109/14756369809036547
– volume: 90
  start-page: 1232
  year: 2010
  ident: 427_CR29
  publication-title: J Sci Food Agric
  doi: 10.1002/jsfa.3958
SSID ssj0000515910
Score 2.048243
Snippet This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed...
SourceID pubmedcentral
proquest
pubmed
crossref
springer
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 113
SubjectTerms Agriculture
arachidonic acid
Bioinformatics
Biomaterials
Biotechnology
Cancer Research
Chemistry
Chemistry and Materials Science
circular dichroism spectroscopy
Enzymes
Fatty acids
Food
isoelectric point
Legumes
linoleate 13S-lipoxygenase
linoleic acid
linolenic acid
molecular weight
mung beans
Original
Original Article
Proteins
seed germination
seedlings
Seeds
Soybeans
Stem Cells
temperature
Vigna radiata
SummonAdditionalLinks – databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfR3LbtNAcETTA70gaKE1BLRIPUCRW3u9fp0qqBpFVYkiRKrcrPXa21oKdogTCf6-M36FEDUXH-xZy96ZnfcD4NT1bR36WppJYElThFZsSklWq0b6SMjzpsk18H3kDSfiZupOG4db2aRVtjyxYtRJochHfoGSCElTeI64nP82aWoURVebERp7sI8sOHB7sP_tejT-0XlZaIIJCsQ2nFnVzDm8yldDQ1pw33Q3BdKWlrmdLPlfxLQSRIOX8KLRINnXGuWv4FmaH8LztsC4PIJsvFpQAlC150zmCVNdV-a66JIVms2yefHnL5IPijFGRSbsF557FqcyZ5_usvtcsgX1LVhKdnv-md3XSTOUJM1KlHhUxV6-hsng-ufV0GwmKpjKdbyl6YS2tlNJwUc7QSzxVKL5pz1UwqStQqVVInXqh1wJpR1baRevQiR4V_k05eoN9PIiT0-AUWkJrgtigTZNaEnJ4ziWlmclXJARYoDVbmukmnbjNPViFq0bJRMmIkoxI0xErgFn3ZJ53WtjF3C_xVXUHLsyWhOJAR-7x3hgKAoi87RYEQxZcYFjBbtgAgv_As3Rp2E4jTdF7sV9A45rEum-Gl-PjDNwDPA3iKcDoKbem0_y7KFq7u06ISppuPJLS2b__N5Tm_F292a8gwNeETw5j_rQWy5W6XvUpZbxh-bAPAK5bB1P
  priority: 102
  providerName: ProQuest
– databaseName: Springer Open Access Hybrid - NESLI2 2011-2012
  dbid: 40G
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1LT9xADLZ4HIBDVSjQtBQNUg88FDSZTF5HhHgIAeoB0N6iyWRmWWmbRZtdCf49dl6wpSBxiaLEEyWxx2OP7c8Av4PIs0lklZvHXLky4ZmrFHmtFuUjp503S1sDV9fh-a286AW9po67bLPd25Bkpalfit18USWaoQcsReQG87BIaGIk1pKfdRsr1LQkqVAIBJVJB5HotdHM_z1ldj16Y2S-zZX8J2BarUOnX-FLY0Cyo5rjqzBnijVYOeqPGxANswZLx20XNzxvK4_LbzD4Mx1TZlDFDKaKnOkOrrmuxmQjy4aDh9HjE8oVrm-Mqk_YX1QILDOqYLt3g36h2JgADSaKXR7usX6dTUPZ06zEpZDK28t1uD09uTk-d5tWC64O_HDi-olnPaMoKunlyD5hFPqFNkTrTHk60VbnypooEVpq63vaBniUMserOqL2VxuwUIwK8x0Y1ZzguDiT6OwkXCmRZZniIc-FJO_EAd7-8FQ3OOTUDmOYviAoE49Syj0jHqWBA_vdkIcahOMj4q2Wi2kzH8sU7RhUbDL0pQM73W1kBYVHVGFGU6Ih9y72efwRTczxK9BPfZ9GUN9TVGsicmCzFp7urfHxqFFj34FoRqw6AkL7nr1TDO4r1O_AT9B6w5EHrQC--rz3fsaPT1H_hGVRzQzaZNqChcl4an6hzTXJtqs59gxggSK5
  priority: 102
  providerName: Springer Nature
Title Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings
URI https://link.springer.com/article/10.1007/s13205-016-0427-5
https://www.ncbi.nlm.nih.gov/pubmed/28330183
https://www.proquest.com/docview/1813054634
https://www.proquest.com/docview/1808628308
https://www.proquest.com/docview/1880467282
https://www.proquest.com/docview/2020863827
https://pubmed.ncbi.nlm.nih.gov/PMC5398193
Volume 6
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1LT9wwEB7BcoBL1ZY-QilyJQ5tUZDj2HkcUEVXbFFVEEJdtLfIcWK60jYL-5CWf89MXnTLQ1wsJRlHiWfsmbFnvgHYVaFn49BqN4u4dmXMU1dr8lotykdGO2-WtgZOToPjvvw5UIMVaMpb1QM4fdC1o3pS_clof3F98w0n_MFdGpwvyhA09I2lCF21CmuomAIS8pPa2q-hvlVc4hMISqBWoRg055wPvWVZU90zP-9HUf53lFpqqN5LeFGbluywkoVXsJIXr2G9yTyebsLwbD6hyKCSGUwXGTMtXHOVjcnGlo2GV-PFDcoV6jdG2SfsLy4ILM11wT5fDC8LzSYEaDDT7Nf-F3ZZRdNQ9DSboiqk9PbpG-j3jn53j9261IJrlB_MXD_2rJdrOpX0MmSfyDX6hTZA60x7JjbWZNrmYSyMNNb3jFXYSpnhXRNS-au30CnGRf4eGOWcYL8olejsxFxrkaap5gHPhCTvxAHeDGtiahxyKocxSu4QlIkTCcWeEScS5cDXtstVBcLxFPF2w6ukEacE7Rhc2GTgSwc-tY9xJtHxiC7y8ZxoyL2LfB49RRNx_Av0Ux-nEVT3FJc1ETrwrhKR9qvx9biiRr4D4ZLwtASE9r38pBj-KVG_lR-j9YY99xox--f3HhuMrWd85QfYEKXU09bSNnRmk3n-ES2tWboDq5L_wDbqYbv2_ej07ByvukF3p5xZ2PbF4S3j3igA
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtR3bTtRA9AThAV-I4q2KMCSaeEmlnU5vD8QIQhZZNsSA4a1OpzO4CbbrdjfKT_mNntMbLoR946UP7ZmmnXOfcwN45YeuiUMj7SxypC1iJ7WlJK_VIH1kdPJm6GjgaBD0TsWXM_9sAf62tTCUVtnKxEpQZ4WiM_It1ERImiLwxMfRL5umRlF0tR2hUZPFob78jS5buX3wGfH7mvP9vZPdnt1MFbCV7wUT24td42pJATg3wy_lWqILZAI0RKSrYmVUJo0OY66EMp6rjI9XITK8q0Ka9ITvvQdLaGbEyEVLO3uD46_dqQ5NTEEF3IZPqxo9j1f5cei4Cx7a_qwCvGHV3kzOvBahrRTf_gNYaSxW9qkmsYewoPNVWG4LmstHMDyejinhqMIxk3nGVNcFui7yZIVhF8NR8ecSyRXVJqOiFvYT5QxLtczZm2_D81yyMfVJmEjW__CWnddJOpSUzUrUsFQ1Xz6G0zvZ6yewmBe5fgaMSllwXZQK9KFiR0qepql0AifjgpweC5x2WxPVtDenKRsXyVVjZsJEQilthInEt-Bdt2RU9_aYB7zW4ipp2LxMrojSgs3uMTIoRV1krospwZDXGHlONA8mcvAv0P29HYbTOFWUljy04GlNIt1X4-tRUEeeBeEM8XQA1ER89kk-_FE1E_e9GI1CXPm-JbP_fu-2zXg-fzM2YLl3ctRP-geDwxdwn1fETwdXa7A4GU_1S7TjJul6wzwMvt81v_4DITZbbg
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Zb9swDCa6FtjxULTd5a3bNGAPO-DWluXrMWgX9FrRh2XImyHLUhqgU4LYAbZ_P9JXm3UtsBfDsCnDNimKFMmPAB_C2DdpbKRbJJ50RerlrpTktRqUj4J23gxtDXw7j45G4mQcjts-p2WX7d6FJJuaBkJpstX-vDD714VvAa-TztAbFjx2wwewgdrYJ-9rxAf9Jgs1MElrRAJOJdNhzMddZPNfT1ldm24ZnLfzJv8KntZr0nALNltjkg0a7m_DmrY78GQwWbSAGnoHHh10Hd3wvKtCLp_C9GK5oCyhmjFM2oKpHrq5qcxkM8OupvPZr98oY7jWMapEYT9RObBcS8s-_phOrGQLAjeoJDvb-8QmTWYNZVKzEpdFKnUvn8Fo-PX7wZHbtl1wVRhElRukvvG1pAilXyAruZboI5oILTXpq1QZVUij45QroUzgKxPiUYgCr6qYWmE9h3U7s_olMKo_wXFJLtDxST0peZ7n0ou8ggvyVBzwuh-eqRaTnFpjXGXXaMrEo4zy0IhHWejA537IvAHkuI94t-Ni1s7NMkObBpWciALhwPv-NrKCQiXS6tmSaMjVSwIvuY8m8fAr0Ge9m4ZTD1RUcTx24EUjPP1b4-NRuyaBA_GKWPUEhPy9esdOL2sE8DBI0ZLDkV86AbzxeXf9jFf_Rf0OHl4cDrOz4_PT1_CY15OE9p52Yb1aLPUbNMWq_G093f4A83wqFA
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Purification+and+characterization+of+lipoxygenase+from+mung+bean+%28Vigna+radiata+L.%29+germinating+seedlings&rft.jtitle=3+Biotech&rft.au=Aanangi%2C+Raveendra&rft.au=Kotapati%2C+Kasi+Viswanath&rft.au=Palaka%2C+Bhagath+Kumar&rft.au=Kedam%2C+Thyagaraju&rft.date=2016-06-01&rft.issn=2190-572X&rft.volume=6&rft.issue=1+p.113-113&rft.spage=113&rft.epage=113&rft_id=info:doi/10.1007%2Fs13205-016-0427-5&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2190-572X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2190-572X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2190-572X&client=summon