Effect of Pyridoxine Deficiency on Ornithine Aminotransferase in Rat Kidney and Liver

The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caus...

Full description

Saved in:
Bibliographic Details
Published inJournal of Nutritional Science and Vitaminology Vol. 31; no. 6; pp. 553 - 561
Main Authors IKEDA, Masuko, OKADA, Mitsuko
Format Journal Article
LanguageEnglish
Published Japan Center for Academic Publications Japan 1985
Subjects
Online AccessGet full text
ISSN0301-4800
1881-7742
DOI10.3177/jnsv.31.553

Cover

Abstract The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.
AbstractList The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.
The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.
The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.
Author IKEDA, Masuko
OKADA, Mitsuko
Author_xml – sequence: 1
  fullname: IKEDA, Masuko
  organization: Department of Food and Nutrition, Kinki University
– sequence: 1
  fullname: OKADA, Mitsuko
  organization: Department of Nutrition, School of Medicine, The University of Tokushima
BackLink https://www.ncbi.nlm.nih.gov/pubmed/3834046$$D View this record in MEDLINE/PubMed
BookMark eNp1kEtLAzEUhYMotT5WroWs3Mho0mRm0qXY-sBCRex6SJMbmzJNNEmL_femtnQhuEkO93znwj0n6NB5BwhdUHLDaF3fzl1cZXVTluwAdakQtKhr3jtEXcIILbgg5BidxDgnhPcFFx3UYYJxwqsumgyNAZWwN_h1Haz239YBHoCxyoJTa-wdHgdn02wzv1tY51OQLhoIMgK2Dr_JhF-sdrDG0mk8sisIZ-jIyDbC-e4_RZOH4fv9UzEaPz7f340KVZIyFf0eED3llOtpX5nKCAYCqlqAlFlqUEYTQ6gmrCS9Suc7ejIfTA0BLQTX7BRdbfd-Bv-1hJiahY0K2lY68MvY1FXFBK3KDF7uwOV0Abr5DHYhw7rZ9ZD9662vgo8xgNkTlDSbkptNyVk1ueRM0z-0skkm613uxrb_ZAbbzDwm-QH7_TIkq1r4ZWm_Zhu-2j45trfVTIYGHPsBKFeZWA
CitedBy_id crossref_primary_10_1016_j_bbapap_2020_140555
crossref_primary_10_1016_S0271_5317_88_80048_4
ContentType Journal Article
Copyright the Center for Academic Publications Japan
Copyright_xml – notice: the Center for Academic Publications Japan
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.3177/jnsv.31.553
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList MEDLINE

MEDLINE - Academic
Database_xml – sequence: 1
  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: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
EISSN 1881-7742
EndPage 561
ExternalDocumentID 3834046
10_3177_jnsv_31_553
article_jnsv1973_31_6_31_6_553_article_char_en
Genre Journal Article
GroupedDBID ---
-~X
.55
.GJ
2WC
3O-
53G
5GY
5RE
AAFWJ
AAWTL
AAYJJ
ADBBV
AENEX
AI.
ALMA_UNASSIGNED_HOLDINGS
BAWUL
C1A
CS3
DIK
DU5
F5P
JSF
JSH
KQ8
OK1
RJT
RZJ
TKC
TR2
VH1
X7J
X7M
ZGI
ZXP
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
PKN
RYR
7X8
ID FETCH-LOGICAL-c505t-92e0db414db9cf6f83e8e678eaa83edecfd0f01d035026d8002a1771f0ed884d3
ISSN 0301-4800
IngestDate Fri Jul 11 05:12:57 EDT 2025
Wed Feb 19 02:36:49 EST 2025
Tue Jul 01 01:41:07 EDT 2025
Thu Apr 24 22:56:06 EDT 2025
Wed Sep 03 06:30:10 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 6
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c505t-92e0db414db9cf6f83e8e678eaa83edecfd0f01d035026d8002a1771f0ed884d3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://www.jstage.jst.go.jp/article/jnsv1973/31/6/31_6_553/_article/-char/en
PMID 3834046
PQID 76638165
PQPubID 23479
PageCount 9
ParticipantIDs proquest_miscellaneous_76638165
pubmed_primary_3834046
crossref_primary_10_3177_jnsv_31_553
crossref_citationtrail_10_3177_jnsv_31_553
jstage_primary_article_jnsv1973_31_6_31_6_553_article_char_en
ProviderPackageCode CITATION
AAYXX
PublicationCentury 1900
PublicationDate 1985-00-00
PublicationDateYYYYMMDD 1985-01-01
PublicationDate_xml – year: 1985
  text: 1985-00-00
PublicationDecade 1980
PublicationPlace Japan
PublicationPlace_xml – name: Japan
PublicationTitle Journal of Nutritional Science and Vitaminology
PublicationTitleAlternate J Nutr Sci Vitaminol
PublicationYear 1985
Publisher Center for Academic Publications Japan
Publisher_xml – name: Center for Academic Publications Japan
References 2) Pitot, H. C., and Peraino, C. (1963): Ornithine b-transaminase in the rat. Biochim. Biophys. Acta, 73, 222-231.
27) Okada, M., and Hirose, M. (1982): Regulation of aspartate amino-transferase activity associated with change of pyridoxal phosphate level. Arch. Biochem. Biophys., 193, 294-300.
37) O'Malley, B. W., and Means, A. R. (1974): Female steroid hormones and target cell nuclei. Science, 183, 610-620.
45) Dolan, K. P., Diaz-Gil, J. J., and Litwack, G. (1980): Interaction of pyridoxal 5'-phosphate with the liver glucocorticoid receptor-DNA complex. Arch. Biochem. Biophys., 201, 476-485.
39) Muller, R. E., Traish, A., Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. I. Inhibition of nuclear binding in cell-free system and intact uterus. J. Biol. Chem., 255, 4062-4067.
1) Katunuma, N., Matsuda, Y., and Tomino, I. (1964): Studies on ornithine-ketoacid transaminase. I. Purification and properties. J. Biochem., 56, 499-503.
33) Gornall, A. G., Bardawill, C. S., and David, M. M. (1949): Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 117, 751-766.
3) Herzfeld, A., and Knox, W. E. (1968): The properties, developmental formation, and estrogen induction of ornithine aminotransferase in rat tissues. ,1. Biol. Chem., 243, 3327-3332.
22) Mueckler, M., and Pitot, H. C. (1983): Regulation of ornithine aminotransferase mRNA levels in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 258, 6109-6114.
21) Wu, C. (1979): Estrogen receptor translocation and ornithine aminotransferase in- duction by estradiol in rat kidney. Biochem. Biophys. Res. Commun., 89, 769-776.
49) Kominami, E., and Katunuma, N. (1976): Studies on new intracellular proteases in various organs of rats. Participation of proteases in degradation of ornithine amino- transferase in vitro and in vivo. Eur. J. Biochem., 62, 425-430.
23) Takami, M., Fujioka, M., Wada, H., and Taguchi, T. (1968): Studies on pyridoxine deficiency in rats. Proc. Soc. Exp. Biol. Med., 129, 110-117.
31) Peraino, C., Bunville, L. G., and Tahmisian, T. N. (1969): Chemical, physical and morphological properties of ornithine aminotransferase from rat liver. J. Biol. Chem., 244, 2241-2249.
40) Traish, A., Muller, R. E., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. II. Inhibition of estrogen receptor transformation. J. Biol. Chem., 255, 4068-4072.
17) Herzferd, A., and Greengard, O. (1969): Endocrine modification of the developmental formation of ornithine aminotransferase in rat tissues. J. Biol. Chem., 244, 4894-4898.
42) Mueller, R. E. Traish, A., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on estrogen receptor activation and nuclear binding. Prog. Cancer Res. Ther.,14, 241-254.
4) Lyons, R. T., and Pitot, H. C. (1976): The regulation of ornithine aminotransferase synthesis by glucagon in the rat. Arch. Biochem. Biophys., 174, 262-272.
32) Strecker, H. J. (1965): The interconversion of glutamic acid and proline. J. Biol. Chem., 240, 1225-1230.
35) Mueckler, M. M., Moran, S., and Pitot, H. C. (1983): Transcriptional control of ornithine aminotransferase synthesis in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 259, 2302-2305.
18) Kobayashi, K., Kito, K., and Katunuma, N. (1976): Effect of estrogen on the turn- over rates of ornithine aminotransferase in rat liver and kidney. J. Biochem., 79, 787- 793.
43) Cake, M. H., DiSorbo, D. M., and Litwack, G. (1978): Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor. J. Biol. Chem., 253, 4886-4891.
13) Bulfield, G., and Hall, J. M. (1981): Ornithine aminotransferase levels in rats and mice differ in their response to oestrogen and testosterone. Comp. Biochem. Physiol., 69B, 295-297.
9) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. I. Inductions of threonine dehydrase and ornithine-5-transaminase by oral intubation of casein hydrolysate. J. Biol. Chem., 239, 1783-1788.
10) Peraino, C., Blake, R. L., and Pitot, H. C. (1965): Studies on the induction and repression of enzymes in rat liver. III. Induction of ornithine-b-transaminase and threonine dehydrase by oral intubation of free amino acids. J. Biol. Chem., 240, 3039-3043.
8) Pitot, H. C., and Peraino, C. (1963): Carbohydrate repression of enzyme induction in rat liver. J. Biol. Chem., 238, 1910-1912.
34) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275.
29) Kondo, T., Nagata, K., Shibuya, M., and Okada, M. (1982): Effect of pyridoxine deficiency on the synthesis of aspartate aminotransferase in rat liver and muscle in vivo. J. Biochem., 92, 1087-1091.
41) Muldoon, T. G., and Cidolowski, J. A. (1980): Specific modification of rat uterine estrogen receptor by pyridoxal 5'-phosphate. J. Biol. Chem., 255, 3100-3107.
19) Lyons, R. T., and Pitot, H. C. (1977): Hormonal regulation of ornithine aminotrans- ferase biosynthesis in rat liver and kidney. Arch. Biochem. Biophys., 180, 472-479.
44) DiSorbo, D. M., Pholps, D. S., Ohl, V. S., and Litwack, G. (1980): Pyridoxal deficiency influences the behavior of the glucocorticoid receptor complex. J. Biol. Chem., 255, 3866-3870.
6) Volpe, P., Menna, T., and Pagano, G. (1974): Ornithine-5-transaminase heterogeneity and regulation. Eur. I Biochem., 44, 455-458.
26) Hunter, J. E., and Happer, A. E. (1976): Stability of some pyridoxal phosphate-dependent enzymes in vitamine Bb deficient rats. J. Nutr., 106, 653-664.
30) Kuroda, K., Hirose, M., and Okada, M. (1982): Increase of inactive form of aspartate aminotransferase in pyridoxine-deficient rat liver. J. Biochem., 92, 1079-1085.
48) Itoh, R., and Okada, M. (1973): Effect of dietary protein level on pyridoxal content in tissues and excretion of pyridoxac acid into urine in normal or pyridoxine-deficient rat. J. Nutr. Sci. Vitaminol., 19, 523-528.
47) Cidlowski, J. A. and Thanassi, J. W. (1978): Extraction of nuclear glucocorticoid receptor complexes with pyridoxal phosphate. Biochem. Biophys. Res. Commun., 82, 1140-1146.
15) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. II. Carbohydrate repression of dietary and hormonal induction of threonine dehydrase and ornithine b-transaminase. J. Biol. Chem., 239, 4308-4313.
28) Shibuya, M., Nagata, K., and Okada, M. (1982): Effect of pyridoxine deficiency on activities and amounts of aspartate aminotransferase isozymes in rat tissues. J. Biochem., 92, 1399-1402.
14) Katunuma, N., Okada, M., Matsuzawa, J., and Otuka, Y. (1965): Studies on ornithine-ketoacid transaminase. II. Role in metabolic pathway. J. Biochem., 57, 445-449.
36) Jensen, E. V., and DeSombre, E. R. (1973): Estrogen receptor interaction. Science, 182, 126-134.
12) Chee, P. Y., and Swick, R. W. (1976): Effect of dietary protein and tryptophan on the turnover of rat liver ornithine aminotransferase. J. Biol. Chem., 251, 1029-1034.
25) Katunuma, N. (1971): Protein, Nucleic Acid and Enzyme (in Japanese), 16, 239-241.
11) Nakajima, K., and Matsuzaka, H. (1970): Hormonal and dietary control of enzymes in the rat. J. Biochem., 67, 779-787.
16) Hunter, J. E., and Harper, A. E. (1977): Induction of pyridoxal phosphate-dependent enzymes in vitamin B6 deficient rat. J. Nutr., 107, 235-244.
46) Cidlowski, J. A., and Thanassi, J. W. (1979): Pyridoxal phosphate induced alterations in glucocorticoid receptor conformation. Biochemistry, 18, 2378-2384.
20) Wu, C. (1978): Estrogen induction of ornithine aminotransferase in rat kidney slices. Biochem. Biophys. Res. Commun., 82, 782-786.
24) Okada, M., and Ochi, A. (1970): The effect of dietary protein level on transaminase activities and fat deposition in vitamin B6-depleted rat liver. J. Biochem., 79, 787-793.
38) Mueller, G. C., Vonderhaar, B., Kim, U. H., and Mahieu, M. L. (1971): Estrogen action: An inroad to cell biology. Recent. Progr. Horm. Res., 21, 1-45.
5) Sanada, Y., Suemori, I., and Katunuma, N. (1970): Properties of ornithine amino- transferase from rat liver, kidney and small intestine. Biochim. Biophys. Acta, 220, 42-50.
7) Kalita, C. C., Kerman, J. D., and Strecker, H. J. (1976): Preparation and properties of ornithine-oxo-acid aminotransferase of rat kidney. Biochim. Biophys. Acta, 429, 780-797.
References_xml – reference: 12) Chee, P. Y., and Swick, R. W. (1976): Effect of dietary protein and tryptophan on the turnover of rat liver ornithine aminotransferase. J. Biol. Chem., 251, 1029-1034.
– reference: 2) Pitot, H. C., and Peraino, C. (1963): Ornithine b-transaminase in the rat. Biochim. Biophys. Acta, 73, 222-231.
– reference: 40) Traish, A., Muller, R. E., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. II. Inhibition of estrogen receptor transformation. J. Biol. Chem., 255, 4068-4072.
– reference: 30) Kuroda, K., Hirose, M., and Okada, M. (1982): Increase of inactive form of aspartate aminotransferase in pyridoxine-deficient rat liver. J. Biochem., 92, 1079-1085.
– reference: 44) DiSorbo, D. M., Pholps, D. S., Ohl, V. S., and Litwack, G. (1980): Pyridoxal deficiency influences the behavior of the glucocorticoid receptor complex. J. Biol. Chem., 255, 3866-3870.
– reference: 43) Cake, M. H., DiSorbo, D. M., and Litwack, G. (1978): Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor. J. Biol. Chem., 253, 4886-4891.
– reference: 29) Kondo, T., Nagata, K., Shibuya, M., and Okada, M. (1982): Effect of pyridoxine deficiency on the synthesis of aspartate aminotransferase in rat liver and muscle in vivo. J. Biochem., 92, 1087-1091.
– reference: 28) Shibuya, M., Nagata, K., and Okada, M. (1982): Effect of pyridoxine deficiency on activities and amounts of aspartate aminotransferase isozymes in rat tissues. J. Biochem., 92, 1399-1402.
– reference: 21) Wu, C. (1979): Estrogen receptor translocation and ornithine aminotransferase in- duction by estradiol in rat kidney. Biochem. Biophys. Res. Commun., 89, 769-776.
– reference: 45) Dolan, K. P., Diaz-Gil, J. J., and Litwack, G. (1980): Interaction of pyridoxal 5'-phosphate with the liver glucocorticoid receptor-DNA complex. Arch. Biochem. Biophys., 201, 476-485.
– reference: 33) Gornall, A. G., Bardawill, C. S., and David, M. M. (1949): Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 117, 751-766.
– reference: 32) Strecker, H. J. (1965): The interconversion of glutamic acid and proline. J. Biol. Chem., 240, 1225-1230.
– reference: 48) Itoh, R., and Okada, M. (1973): Effect of dietary protein level on pyridoxal content in tissues and excretion of pyridoxac acid into urine in normal or pyridoxine-deficient rat. J. Nutr. Sci. Vitaminol., 19, 523-528.
– reference: 18) Kobayashi, K., Kito, K., and Katunuma, N. (1976): Effect of estrogen on the turn- over rates of ornithine aminotransferase in rat liver and kidney. J. Biochem., 79, 787- 793.
– reference: 31) Peraino, C., Bunville, L. G., and Tahmisian, T. N. (1969): Chemical, physical and morphological properties of ornithine aminotransferase from rat liver. J. Biol. Chem., 244, 2241-2249.
– reference: 5) Sanada, Y., Suemori, I., and Katunuma, N. (1970): Properties of ornithine amino- transferase from rat liver, kidney and small intestine. Biochim. Biophys. Acta, 220, 42-50.
– reference: 36) Jensen, E. V., and DeSombre, E. R. (1973): Estrogen receptor interaction. Science, 182, 126-134.
– reference: 4) Lyons, R. T., and Pitot, H. C. (1976): The regulation of ornithine aminotransferase synthesis by glucagon in the rat. Arch. Biochem. Biophys., 174, 262-272.
– reference: 42) Mueller, R. E. Traish, A., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on estrogen receptor activation and nuclear binding. Prog. Cancer Res. Ther.,14, 241-254.
– reference: 22) Mueckler, M., and Pitot, H. C. (1983): Regulation of ornithine aminotransferase mRNA levels in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 258, 6109-6114.
– reference: 41) Muldoon, T. G., and Cidolowski, J. A. (1980): Specific modification of rat uterine estrogen receptor by pyridoxal 5'-phosphate. J. Biol. Chem., 255, 3100-3107.
– reference: 46) Cidlowski, J. A., and Thanassi, J. W. (1979): Pyridoxal phosphate induced alterations in glucocorticoid receptor conformation. Biochemistry, 18, 2378-2384.
– reference: 3) Herzfeld, A., and Knox, W. E. (1968): The properties, developmental formation, and estrogen induction of ornithine aminotransferase in rat tissues. ,1. Biol. Chem., 243, 3327-3332.
– reference: 10) Peraino, C., Blake, R. L., and Pitot, H. C. (1965): Studies on the induction and repression of enzymes in rat liver. III. Induction of ornithine-b-transaminase and threonine dehydrase by oral intubation of free amino acids. J. Biol. Chem., 240, 3039-3043.
– reference: 26) Hunter, J. E., and Happer, A. E. (1976): Stability of some pyridoxal phosphate-dependent enzymes in vitamine Bb deficient rats. J. Nutr., 106, 653-664.
– reference: 13) Bulfield, G., and Hall, J. M. (1981): Ornithine aminotransferase levels in rats and mice differ in their response to oestrogen and testosterone. Comp. Biochem. Physiol., 69B, 295-297.
– reference: 27) Okada, M., and Hirose, M. (1982): Regulation of aspartate amino-transferase activity associated with change of pyridoxal phosphate level. Arch. Biochem. Biophys., 193, 294-300.
– reference: 39) Muller, R. E., Traish, A., Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. I. Inhibition of nuclear binding in cell-free system and intact uterus. J. Biol. Chem., 255, 4062-4067.
– reference: 16) Hunter, J. E., and Harper, A. E. (1977): Induction of pyridoxal phosphate-dependent enzymes in vitamin B6 deficient rat. J. Nutr., 107, 235-244.
– reference: 25) Katunuma, N. (1971): Protein, Nucleic Acid and Enzyme (in Japanese), 16, 239-241.
– reference: 14) Katunuma, N., Okada, M., Matsuzawa, J., and Otuka, Y. (1965): Studies on ornithine-ketoacid transaminase. II. Role in metabolic pathway. J. Biochem., 57, 445-449.
– reference: 6) Volpe, P., Menna, T., and Pagano, G. (1974): Ornithine-5-transaminase heterogeneity and regulation. Eur. I Biochem., 44, 455-458.
– reference: 34) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275.
– reference: 37) O'Malley, B. W., and Means, A. R. (1974): Female steroid hormones and target cell nuclei. Science, 183, 610-620.
– reference: 17) Herzferd, A., and Greengard, O. (1969): Endocrine modification of the developmental formation of ornithine aminotransferase in rat tissues. J. Biol. Chem., 244, 4894-4898.
– reference: 49) Kominami, E., and Katunuma, N. (1976): Studies on new intracellular proteases in various organs of rats. Participation of proteases in degradation of ornithine amino- transferase in vitro and in vivo. Eur. J. Biochem., 62, 425-430.
– reference: 20) Wu, C. (1978): Estrogen induction of ornithine aminotransferase in rat kidney slices. Biochem. Biophys. Res. Commun., 82, 782-786.
– reference: 24) Okada, M., and Ochi, A. (1970): The effect of dietary protein level on transaminase activities and fat deposition in vitamin B6-depleted rat liver. J. Biochem., 79, 787-793.
– reference: 9) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. I. Inductions of threonine dehydrase and ornithine-5-transaminase by oral intubation of casein hydrolysate. J. Biol. Chem., 239, 1783-1788.
– reference: 23) Takami, M., Fujioka, M., Wada, H., and Taguchi, T. (1968): Studies on pyridoxine deficiency in rats. Proc. Soc. Exp. Biol. Med., 129, 110-117.
– reference: 11) Nakajima, K., and Matsuzaka, H. (1970): Hormonal and dietary control of enzymes in the rat. J. Biochem., 67, 779-787.
– reference: 38) Mueller, G. C., Vonderhaar, B., Kim, U. H., and Mahieu, M. L. (1971): Estrogen action: An inroad to cell biology. Recent. Progr. Horm. Res., 21, 1-45.
– reference: 7) Kalita, C. C., Kerman, J. D., and Strecker, H. J. (1976): Preparation and properties of ornithine-oxo-acid aminotransferase of rat kidney. Biochim. Biophys. Acta, 429, 780-797.
– reference: 8) Pitot, H. C., and Peraino, C. (1963): Carbohydrate repression of enzyme induction in rat liver. J. Biol. Chem., 238, 1910-1912.
– reference: 19) Lyons, R. T., and Pitot, H. C. (1977): Hormonal regulation of ornithine aminotrans- ferase biosynthesis in rat liver and kidney. Arch. Biochem. Biophys., 180, 472-479.
– reference: 35) Mueckler, M. M., Moran, S., and Pitot, H. C. (1983): Transcriptional control of ornithine aminotransferase synthesis in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 259, 2302-2305.
– reference: 15) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. II. Carbohydrate repression of dietary and hormonal induction of threonine dehydrase and ornithine b-transaminase. J. Biol. Chem., 239, 4308-4313.
– reference: 1) Katunuma, N., Matsuda, Y., and Tomino, I. (1964): Studies on ornithine-ketoacid transaminase. I. Purification and properties. J. Biochem., 56, 499-503.
– reference: 47) Cidlowski, J. A. and Thanassi, J. W. (1978): Extraction of nuclear glucocorticoid receptor complexes with pyridoxal phosphate. Biochem. Biophys. Res. Commun., 82, 1140-1146.
SSID ssj0049848
Score 1.2760868
Snippet The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female...
The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female...
SourceID proquest
pubmed
crossref
jstage
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 553
SubjectTerms Animals
Antigens, Surface - analysis
Female
hepatic and renal OAT
Kidney - enzymology
Kidney - immunology
Kidney - metabolism
Liver - enzymology
Liver - immunology
Liver - metabolism
Male
Membrane Proteins
Ornithine-Oxo-Acid Transaminase - metabolism
Protein Biosynthesis
Proteins - analysis
pyridoxal phosphate
pyridoxine deficiency
Rats
Rats, Inbred Strains
Sex Factors
sexual difference
synthesis of OAT
Transaminases - metabolism
Vitamin B 6 Deficiency - enzymology
Title Effect of Pyridoxine Deficiency on Ornithine Aminotransferase in Rat Kidney and Liver
URI https://www.jstage.jst.go.jp/article/jnsv1973/31/6/31_6_553/_article/-char/en
https://www.ncbi.nlm.nih.gov/pubmed/3834046
https://www.proquest.com/docview/76638165
Volume 31
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
ispartofPNX Journal of Nutritional Science and Vitaminology, 1985, Vol.31(6), pp.553-561
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3Pb9MwFLbK4MBlAsZE-enDxAGUkdRO4hw4RHRoW2FIaEW7RU5sQ8bmoDZFjH-Cf5n34iRrxyYxuFiW68Spv8_Pz_Z7z4RsGZ4bFqvcM4IpvMIs9xIxCryw0DIxmhe-wn3I9wfR7pTvH4VHg8GvJaulRZ1vFz8v9Sv5F1ShDHBFL9lrINu_FAogD_hCCghD-lcYt6GH0YztbFaq6geqjGONQSEaj0pA9sMMxuwXLE9PS1vVjZ6qZzB34U7HR1m_nJTKaheF6R0aaVyhrh50Yfvb8CGdp8Gnspb45uXd-b3Jzjh1nkDzxdeq38idpG1xWfflyrnguRt1nMkPhgmdNfaPq9b7neH7PkzwdkmCgfTwuPDdwYt2ElaIAFR6viKC24mg_EOehi6ScDs1hy5u-0Wpz9y587Gdf4f8dv_MShjtFqQMawVJzDIWZJFL4IGs-xl93YBaN8jNURwHaCM63pt0UztPRHMdW_-_nMMntv9qqfUVFefWMWj5n_XVC5hGkTm8Q9ZbSGnqPuUuGWh7j2ykVtbV6Rl9Thub4AbODTJ1DKOVoecMo-cMo5WlPcPoRYbR0lJgGHUMo8AW2jDsPpm-3Tl8s-u1F3F4BSjItZeMtK9yHnCVJ4WJYFhroUHL0VJCVunCKN_4gcJT6lGkcA0ioU8C42slBFdsk6zZyuoHhJow50YnifSV4izXIlE61jAlCyZzyfiQvOj6LivaKPV4WcpJBqtV7OgGQMQNOnpItvrK31xwlsurvXYg9JWuR4YhedZhl4HwxRM1aXW1mGcx6OsiiMIh2XSQ9i0wwbjPo4f_2fQjchtHoNvze0zW6tlCPwEtuM6fNsz8DTcqvZo
linkProvider Flying Publisher
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=Effect+of+Pyridoxine+Deficiency+on+Ornithine+Aminotransferase+in+Rat+Kidney+and+Liver&rft.jtitle=Journal+of+Nutritional+Science+and+Vitaminology&rft.au=IKEDA%2C+Masuko&rft.au=OKADA%2C+Mitsuko&rft.date=1985&rft.pub=Center+for+Academic+Publications+Japan&rft.issn=0301-4800&rft.eissn=1881-7742&rft.volume=31&rft.issue=6&rft.spage=553&rft.epage=561&rft_id=info:doi/10.3177%2Fjnsv.31.553&rft.externalDocID=article_jnsv1973_31_6_31_6_553_article_char_en
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0301-4800&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0301-4800&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0301-4800&client=summon