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1
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Biochem J. 1978 Nov 1;175(2):765-8. doi: 10.1042/bj1750765.
2
Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species.不同哺乳动物物种中肝脏丙氨酸-乙醛酸氨基转移酶的特征
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本文引用的文献

1
The subcellular distribution of rat liver L-alanine-glyoxylate aminotransferase in relation to a pathway for glucose formation involving glyoxylate.大鼠肝脏L-丙氨酸-乙醛酸氨基转移酶的亚细胞分布与涉及乙醛酸的葡萄糖生成途径的关系。
Biochem J. 1972 Mar;127(1):155-65. doi: 10.1042/bj1270155.
2
Isolation and properties of a new glutamine transaminase from rat kidney.
J Biol Chem. 1974 Apr 25;249(8):2554-61.
3
Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat.新生大鼠发育过程中肝脏L-丝氨酸脱水酶和L-丝氨酸-丙酮酸转氨酶的调节
Biochem J. 1974 Dec;144(3):519-31. doi: 10.1042/bj1440519.
4
The adaptive behaviour of isoenzyme forms of rat liver alanine aminotransferases during development.大鼠肝脏丙氨酸转氨酶同工酶形式在发育过程中的适应性行为。
Biochem J. 1972 Jun;128(2):403-13. doi: 10.1042/bj1280403.
5
Purification, characterization and identification of rat liver histidine-pyruvate aminotransferase isoenzymes.大鼠肝脏组氨酸-丙酮酸转氨酶同工酶的纯化、表征及鉴定
Biochem J. 1976 Apr 1;155(1):107-15. doi: 10.1042/bj1550107.
6
Glyoxylate aminotransferase in peroxisomes from rat liver and kidney.大鼠肝脏和肾脏过氧化物酶体中的乙醛酸转氨酶。
J Biol Chem. 1976 Jul 25;251(14):4408-15.
7
Characteristics of hepatic serine-pyruvate aminotransferase in different mammalian species.不同哺乳动物物种中肝脏丝氨酸-丙酮酸转氨酶的特征
Biochem J. 1977 Mar 1;161(3):609-14. doi: 10.1042/bj1610609.
8
Identity of rat kidney histidine-pyruvate aminotransferase with glutamine-oxo acid aminotransferase.大鼠肾组氨酸-丙酮酸氨基转移酶与谷氨酰胺-氧代酸氨基转移酶的同一性。
Biochem J. 1977 Jan 1;161(1):177-9. doi: 10.1042/bj1610177.
9
Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species.不同哺乳动物物种中肝脏丙氨酸-乙醛酸氨基转移酶的特征
Biochem J. 1978 Jan 1;169(1):113-22. doi: 10.1042/bj1690113.
10
Subcellular distribution of pyruvate (glyoxylate) aminotransferases in rat liver.大鼠肝脏中丙酮酸（乙醛酸）氨基转移酶的亚细胞分布
Biochem J. 1978 Jan 15;170(1):173-5. doi: 10.1042/bj1700173.

大鼠肝脏过氧化物酶体丙酮酸（乙醛酸）氨基转移酶的纯化及性质

Purification and properties of peroxisomal pyruvate (glyoxylate) aminotransferase from rat liver.

作者信息

Noguchi T, Takada Y

出版信息

Biochem J. 1978 Nov 1;175(2):765-8. doi: 10.1042/bj1750765.

DOI:10.1042/bj1750765
PMID:743224
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1186129/
Abstract

Pyruvate (glyoxylate) aminotransferase from rat liver peroxisomes was highly purified and characterized. The enzyme preparation has a mol.wt. of approx. 80,000 with two identical subunits, and isoelectric point of 8.0 and a pH optimum between 8.0 and 8.5. The enzyme catalysed transamination between a number of L-amino acids and pyruvate or glyoxylate. The effective amino acceptors were pyruvate, phenylpyruvate and glyoxylate with serine, and glyoxylate and phenylpyruvate with alanine as amino donor. These properties and kinetic parameters of the enzyme are remarkably similar to those previously described for mitochondrial alanine-glyoxylate aminotransferase isoenzyme 1 from glucagon-injected rat liver [Noguchi, Okuno, Takada, Minatogawa, Okai & Kido (1978, Biochem. J. 169, 113-122].

摘要

对来自大鼠肝脏过氧化物酶体的丙酮酸（乙醛酸）转氨酶进行了高度纯化和表征。该酶制剂的分子量约为80,000，有两个相同的亚基，等电点为8.0，最适pH在8.0至8.5之间。该酶催化多种L-氨基酸与丙酮酸或乙醛酸之间的转氨作用。有效的氨基受体是丙酮酸、苯丙酮酸和乙醛酸与丝氨酸，以及乙醛酸和苯丙酮酸与丙氨酸作为氨基供体。该酶的这些性质和动力学参数与先前描述的来自注射胰高血糖素的大鼠肝脏的线粒体丙氨酸-乙醛酸转氨酶同工酶1非常相似[野口、奥野、高田、皆藤川、冈井和木户（1978年，《生物化学杂志》169，113 - 122）]。