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.
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）]。
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