Apoprotein Composition and Spectroscopic Characterization of the Water-Soluble Peridinin--Chlorophyll a--Proteins from Three Symbiotic Dinoflagellates

The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption an...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the Royal Society. B, Biological sciences Vol. 246; no. 1317; pp. 275 - 283
Main Authors Iglesias-Prieto, R., Govind, N. S., Trench, R. K.
Format Journal Article
LanguageEnglish
Published London The Royal Society 23.12.1991
Subjects
Online AccessGet full text
ISSN0962-8452
1471-2954
DOI10.1098/rspb.1991.0155

Cover

Loading…
Abstract The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S.microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum', sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose m olecular topologies for sPCP consistent with our findings.
AbstractList The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S. microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum; sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose molecular topologies for sPCP consistent with our findings.
The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S.microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum', sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose m olecular topologies for sPCP consistent with our findings.
The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S. microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum; sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose molecular topologies for sPCP consistent with our findings.
Author Govind, N. S.
Trench, R. K.
Iglesias-Prieto, R.
Author_xml – sequence: 1
  givenname: R.
  surname: Iglesias-Prieto
  fullname: Iglesias-Prieto, R.
  organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A
– sequence: 2
  givenname: N. S.
  surname: Govind
  fullname: Govind, N. S.
  organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A
– sequence: 3
  givenname: R. K.
  surname: Trench
  fullname: Trench, R. K.
  organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A
BookMark eNp9UN1u0zAUjtCQ6Aa3XHCVF0ixEzuOr9BIx0CaoKJjSNxYjuMsLm5s2S7QPQjPi5OgSQVtV9bx93fOd5qcDGaQSfISgiUEtHrtvG2WkFK4BBDjJ8kCIgKznGJ0kiwALfOsQjh_lpx6vwUAUFzhRfL73BrrTJBqSGuzs8aroMyQ8qFNN1aK4IwXxiqR1j13XATp1B2fKKZLQy_Trzz-ZRuj942W6TrirRrUkGV1r40ztj9onfIsW88pPu2c2aXXvZMy3Rx2jTIhuq_UYDrNb6XW0c8_T552XHv54u97lnx5d3Fdv8-uPl1-qM-vMoEwDVmZFwTwoiG4RQQVpIQUVQ3OOYa0hBC1ZU54S5pGYgJAU1IgRMsbStpcRkQWZ8ly9hXxTu9kx6xTO-4ODAI2tsrGVtnYKhtbjQL0j0CoMPURHFf6YVkxy5w5xHuMUDIc2Nbs3RDHh1X-MdXnzfptJIMfOSoVLCBhoCogIJDkiN0pO9mNBBYJTHm_l2yiHcf8n_pqTt36YNx9IaQkaASzGVQ-yF_3IHffWUkKgtlNhdjqG7oEK3TDPkY-nPm9uu1_KifZ0S1xsM4304LTajkZM948qhnXFbFwOYQjIev2WjPbdsUfCYb5Gg
CitedBy_id crossref_primary_10_1007_BF00023563
crossref_primary_10_1007_s11120_005_2067_1
crossref_primary_10_1016_j_jbbm_2004_12_004
crossref_primary_10_1126_science_272_5269_1788
crossref_primary_10_1016_j_bbabio_2014_03_019
crossref_primary_10_1016_j_margen_2017_08_010
crossref_primary_10_1007_s11120_022_00951_6
crossref_primary_10_1007_s11120_019_00688_9
crossref_primary_10_1016_S0006_3495_00_76422_8
crossref_primary_10_1529_biophysj_104_055350
crossref_primary_10_3389_fmars_2021_727206
crossref_primary_10_3390_jmse9121387
crossref_primary_10_1111_j_0022_3646_1997_00044_x
crossref_primary_10_1007_s00338_012_0914_z
crossref_primary_10_1016_S0176_1617_96_80326_9
crossref_primary_10_1371_journal_pone_0047456
crossref_primary_10_1098_rstb_1993_0080
crossref_primary_10_1016_j_bbabio_2012_03_027
crossref_primary_10_1111_j_0022_3646_1994_00316_x
crossref_primary_10_3389_fmars_2017_00365
crossref_primary_10_3389_fmars_2023_1048346
crossref_primary_10_3389_fmicb_2014_00422
crossref_primary_10_1016_j_bbabio_2014_07_023
crossref_primary_10_1007_s00338_008_0444_x
crossref_primary_10_1007_BF00346424
crossref_primary_10_3389_fmars_2022_817312
crossref_primary_10_1046_j_1529_8817_2002_01132_x
crossref_primary_10_1016_j_jembe_2004_05_015
crossref_primary_10_1007_PL00022067
crossref_primary_10_3390_ijms24021735
Cites_doi 10.1098/rspb.1982.0037
10.2172/7339260
10.1111/j.1529-8817.1987.tb02534.x
10.1098/rspb.1984.0063
10.1137/0111030
10.1016/0005-2728(90)90070-K
10.1111/j.1529-8817.1987.tb02528.x
10.1104/pp.88.3.594
10.1007/BF00392906
10.1016/0014-5793(80)80307-3
10.1007/BF00387826
10.1098/rspb.1971.0025
10.1038/350130a0
10.1007/978-94-009-2823-7_26
10.1021/bi00665a012
10.1111/j.1751-1097.1979.tb07375.x
10.1104/pp.83.4.805
10.1073/pnas.75.4.1801
10.1104/pp.57.2.297
10.1104/pp.49.3.421
10.1016/1011-1344(90)85112-A
10.1111/j.1751-1097.1970.tb06077.x
10.1098/rspb.1990.0033
10.1111/j.1751-1097.1979.tb07835.x
ContentType Journal Article
Copyright Copyright 1991 The Royal Society
Scanned images copyright © 2017, Royal Society
Copyright_xml – notice: Copyright 1991 The Royal Society
– notice: Scanned images copyright © 2017, Royal Society
DBID BSCLL
AAYXX
CITATION
DOI 10.1098/rspb.1991.0155
DatabaseName Istex
CrossRef
DatabaseTitle CrossRef
DatabaseTitleList



DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
Biology
EISSN 1471-2954
EndPage 283
ExternalDocumentID 10_1098_rspb_1991_0155
76745
ark_67375_V84_DZ4G0D4V_N
royprsb_246_1317_275
GroupedDBID -
02
08R
0R
0VX
36Y
3O-
4.4
53G
55
5RE
85S
8WZ
A6W
ABBHK
ABEFU
ABFLS
ABPTK
ACIWK
ACMKX
ACNCT
ACPRK
ADBBV
ADBIT
ADULT
ADZLD
AEUPB
AFRAH
ALMA_UNASSIGNED_HOLDINGS
AS
BGBPD
COF
CS3
DCCCD
DIK
DNJUQ
DOOOF
DWIUU
EBS
EJD
F5P
FRP
GJ
H13
HGD
HQ3
HTVGU
HZ
JLS
JPM
JSG
JSODD
JST
K-O
KQ8
MVM
O9-
OP1
RHF
RPM
RRY
SA0
V1E
X
X7M
ZXP
---
-~X
.55
.GJ
0R~
AACGO
AANCE
AANZV
ABIEJ
ABPLY
ABTLG
ABXSQ
ACQIA
ADACV
ADIYS
AEXZC
AJZGM
ALMYZ
AQVQM
AS~
BSCLL
BTFSW
HZ~
IPSME
JAAYA
JBMMH
JENOY
JHFFW
JKQEH
JLXEF
MRS
OK1
~02
ACHIC
ACRPL
ADNMO
ADQXQ
AGPVY
AGQPQ
AEQTP
AAYXX
CITATION
ID FETCH-LOGICAL-c459t-62370a3b75d4743761948b52a5196114d627ad7bbe5700b690ccdab97d2e27ae3
ISSN 0962-8452
IngestDate Tue Jul 01 00:46:32 EDT 2025
Thu Apr 24 22:51:17 EDT 2025
Wed Jan 17 02:37:12 EST 2024
Tue May 24 16:19:19 EDT 2022
Thu Jul 03 21:38:11 EDT 2025
Wed Oct 30 10:00:25 EDT 2024
Tue Jan 05 21:30:10 EST 2021
Mon May 06 10:48:28 EDT 2019
IsPeerReviewed true
IsScholarly true
Issue 1317
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c459t-62370a3b75d4743761948b52a5196114d627ad7bbe5700b690ccdab97d2e27ae3
Notes ark:/67375/V84-DZ4G0D4V-N
istex:FA9EC6588E0DC43EDA0C0AA5127E52E7ED2D3CFA
This text was harvested from a scanned image of the original document using optical character recognition (OCR) software. As such, it may contain errors. Please contact the Royal Society if you find an error you would like to see corrected. Mathematical notations produced through Infty OCR.
PageCount 9
ParticipantIDs royalsociety_journals_RSPB1990v246i1317_0831071724_zip_rspb1990_246_issue_1317_rspb_1991_0155_rspb_1991_0155
istex_primary_ark_67375_V84_DZ4G0D4V_N
crossref_primary_10_1098_rspb_1991_0155
jstor_primary_76745
crossref_citationtrail_10_1098_rspb_1991_0155
royalsociety_journals_10_1098_rspb_1991_0155
highwire_royalsociety_royprsb_246_1317_275
ProviderPackageCode RHF
CITATION
AAYXX
PublicationCentury 1900
PublicationDate 19911223
PublicationDateYYYYMMDD 1991-12-23
PublicationDate_xml – month: 12
  year: 1991
  text: 19911223
  day: 23
PublicationDecade 1990
PublicationPlace London
PublicationPlace_xml – name: London
PublicationTitle Proceedings of the Royal Society. B, Biological sciences
PublicationTitleAbbrev Proc. R. Soc. Lond. B
PublicationTitleAlternate Proc. R. Soc. Lond. B
PublicationYear 1991
Publisher The Royal Society
Publisher_xml – name: The Royal Society
References p_27
p_28
Hiller R. G. (p_15) 1988; 932
p_29
Larkum A. W. (p_20) 1983; 10
Koka P. (p_18) 1977; 495
p_23
p_25
p_26
Mimuro M. (p_24) 1990; 1015
Tronrud D. E. (p_38) 1986; 188
Matthews B. W. (p_22) 1979; 131
p_21
Brown J. S. (p_5) 1981; 636
Boczar B. A. (p_3) 1986; 850
p_17
p_39
p_2
p_1
Dorssen (p_9) 1987; 890
p_19
p_4
p_12
p_34
p_13
p_35
p_6
p_14
p_36
p_37
p_8
Jennings R. C. (p_16) 1990; 1016
p_7
Shiozawa J. A. (p_31) 1974; 165
p_30
p_10
p_32
p_11
p_33
References_xml – ident: p_7
  doi: 10.1098/rspb.1982.0037
– ident: p_33
  doi: 10.2172/7339260
– ident: p_37
  doi: 10.1111/j.1529-8817.1987.tb02534.x
– ident: p_8
  doi: 10.1098/rspb.1984.0063
– ident: p_17
– ident: p_21
  doi: 10.1137/0111030
– volume: 1015
  start-page: 450
  year: 1990
  ident: p_24
  article-title: 7? Spatial arrangement of pigments and their interaction in the fucoxanthin-chlorophyll a/c protein assembly (fcpa) isolated from the brown alga Dictyota dichotoma. Analysis by means of polarized spectroscopy. Biochim. biophys
  publication-title: Acta
– volume: 636
  start-page: 201
  year: 1981
  ident: p_5
  article-title: Spectral analysis of chlorophyll-protein complexes from higher plant chloroplasts. Biochim. biophys
  publication-title: Acta
– ident: p_23
  doi: 10.1016/0005-2728(90)90070-K
– ident: p_11
  doi: 10.1111/j.1529-8817.1987.tb02528.x
– ident: p_36
– ident: p_29
  doi: 10.1104/pp.88.3.594
– ident: p_1
  doi: 10.1007/BF00392906
– ident: p_26
– ident: p_2
  doi: 10.1016/0014-5793(80)80307-3
– ident: p_27
  doi: 10.1007/BF00387826
– ident: p_35
  doi: 10.1098/rspb.1971.0025
– volume: 890
  start-page: 134
  year: 1987
  ident: p_9
  article-title: Spectroscopic properties of chloroplast grana membranes of the core of photosystem II. Biochem. biophys
  publication-title: Acta
– ident: p_19
  doi: 10.1038/350130a0
– ident: p_30
  doi: 10.1007/978-94-009-2823-7_26
– ident: p_34
  doi: 10.1021/bi00665a012
– ident: p_13
  doi: 10.1111/j.1751-1097.1979.tb07375.x
– volume: 10
  start-page: 3
  year: 1983
  ident: p_20
  article-title: Light-harvesting processes in algae. Adv. hot
  publication-title: Res.
– volume: 495
  start-page: 220
  year: 1977
  ident: p_18
  article-title: The chromophore topography and the binding environment of peridinin-chlorophyll a-protein complexes from marine dinoflagellate algae. Biochim. biophys
  publication-title: Acta
– ident: p_4
  doi: 10.1104/pp.83.4.805
– ident: p_28
  doi: 10.1073/pnas.75.4.1801
– ident: p_14
  doi: 10.1104/pp.57.2.297
– volume: 131
  start-page: 259
  year: 1979
  ident: p_22
  article-title: Structure of bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii. J. molec
  publication-title: Biol.
– volume: 188
  start-page: 443
  year: 1986
  ident: p_38
  article-title: Structure and X-ray amino acid sequence of a bacteriochlorof)hyll a protein from Prosthecochloris aestuarii refined at 1.9 A resolution. J. molec
  publication-title: Biol.
– volume: 932
  start-page: 223
  year: 1988
  ident: p_15
  article-title: Chlorophyll-proteins of the prym-nesiophyte Pavlova lutherii (Droop) com. nov.: identification of the major lightharvesting complex. Biochim. biophys
  publication-title: Acta
– ident: p_25
– ident: p_10
  doi: 10.1104/pp.49.3.421
– volume: 165
  start-page: 338
  year: 1974
  ident: p_31
  article-title: The P700 chlorophyll a-protein. Isolation and some characteristics of the complex in higher plants
  publication-title: Archs Biochem. Biophys.
– ident: p_39
  doi: 10.1016/1011-1344(90)85112-A
– volume: 1016
  start-page: 259
  year: 1990
  ident: p_16
  article-title: Excitation energy transfer from the chlorophyll spectral forms to photosystem II reaction centres: a fluorescence induction study. Biochim. biophys
  publication-title: Acta
– ident: p_6
  doi: 10.1111/j.1751-1097.1970.tb06077.x
– ident: p_12
  doi: 10.1098/rspb.1990.0033
– ident: p_32
  doi: 10.1111/j.1751-1097.1979.tb07835.x
– volume: 850
  start-page: 300
  year: 1986
  ident: p_3
  article-title: Light and MgCl 2- dependent characteristics of four chlorophyll-protein complexes isolated from the marine dinoflagellate Glenodinium sp. Biochim. biophys
  publication-title: Acta
SSID ssj0009585
Score 1.5511247
Snippet The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum,...
The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum,...
The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum,...
SourceID crossref
royalsociety
jstor
istex
highwire
SourceType Enrichment Source
Index Database
Publisher
StartPage 275
SubjectTerms Absorption spectra
Apoproteins
Chlorophylls
Emission spectra
Fluorescence
Molecules
Room temperature
Spectroscopic analysis
Spectroscopy
Symbiosis
Title Apoprotein Composition and Spectroscopic Characterization of the Water-Soluble Peridinin--Chlorophyll a--Proteins from Three Symbiotic Dinoflagellates
URI http://rspb.royalsocietypublishing.org/content/246/1317/275.abstract
https://api.istex.fr/ark:/67375/V84-DZ4G0D4V-N/fulltext.pdf
https://www.jstor.org/stable/76745
https://royalsocietypublishing.org/doi/full/10.1098/rspb.1991.0155
Volume 246
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELZKERIXRBcQy0s-IF5LQpJ1NsmxpUChoip9qeJixXECK5ZulGyB9sSP4MDvQ-J_MGM73qS0EuWy2nhnbSfzZTxjz4OQ-8O0AMGYMKeQYJswmRWOyIe5k4ZxzkSUhIxhvPPbjdHaLnuzH-4vLPxueS0dzoSbHZ8aV_I_XIU24CtGyZ6Ds7ZTaIDvwF_4BA7D5z_xeLmcqjwLxpfc-F-p8wAVQYmZKqflOMPwXpOW-diqiKhxfgVNs3JwkhhAhUmPJRaMaDwgWPYRzPkpcGIyGaS21YxZN7EpVZ4P6qPPYjzF7K_Qw7SYgJgCgM2Mh6LRfjftalk3M9DbF8Z31B2sKLyNrUQ2C7RV_F9_mOT1OK2dTTDxVQWowZZrfYhwd0Tq-LHBtm1Gt19d8GrLHay7830O5Y_lB44ORXabSLnOlNpbmSOQ6kxnwnVzLchh0XXwDLMt6QOz22kgPdRRo43o1hVcjBYQ6PI6fy0wXoJBE1VdCozz9F1UOedLqXVw1Ef7MUdCjoQcCS-QiwFYM7h-rL-LW7mhVeVYexs2t2j8rDtQV3dq8lmDWYUS4VvjUQsqVIUPqtbPqaUu7VwlV4ydQ5c1aJfIQn7QI5c0Z496ZMmsKTV9ZBKfP75Gfs7xTFt4poBn2sEzPYlnOi0ooIl28Ewtnn99_9FCMk3husEwRQxThWFqMUxPYPg62X35Yuf5mmMqhzgZC5OZAzp95KVDEYWSgYqstupiEQYp2Csj32dyFESpjITIsbyDGCVelslUJJEMcvglH94giwfTg_wmoVlS-H6UetKTIUsKWO6KTAY-S8F08j0p-sRpeMIzk1Yfq7tM-OkY6JOHlr7UCWXOpHzSsJi3GYoXZVULDnDmCGIO0O2T-Axi7BPDXrBod_sfHM_3eCmLPnmg8GOnk1af0N0TSPZixlffs1feKtvjG33SUwCzhJgIDEZ-2hnQyMf6zLuanE6-tb25AlTeF5jkWE1SFUGMwMJi_Hhcqn6QQN2FeoX1vXT7P3F563yzu00uz2XPHbI4qw7zu2B1zMQ99c7-ASgENtg
linkProvider Colorado Alliance of Research Libraries
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=Apoprotein+composition+and+spectroscopic+characterization+of+the+water-soluble+peridinin%E2%80%94chlorophyll+a%E2%80%94proteins+from+three+symbiotic+dinoflagellates&rft.jtitle=Proceedings+of+the+Royal+Society.+B%2C+Biological+sciences&rft.au=Iglesias-Prieto%2C+R.&rft.au=Govind%2C+N.+S.&rft.au=Trench%2C+R.+K.&rft.date=1991-12-23&rft.pub=The+Royal+Society&rft.issn=0962-8452&rft.eissn=1471-2954&rft.volume=246&rft.issue=1317&rft.spage=275&rft.epage=283&rft_id=info:doi/10.1098%2Frspb.1991.0155&rft.externalDocID=10_1098_rspb_1991_0155
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0962-8452&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0962-8452&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0962-8452&client=summon