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鸡肝L-2-羟基酸氧化酶A的纯化及某些特性

Purification and some characteristics of chicken liver L-2-hydroxyacid oxidase A.

作者信息

Dupuis L, De Caro J, Brachet P, Puigserver A

机构信息

Centre de Biochimie et de Biologie Moléculaire du Centre National de la Recherche Scientifique, Marseille, France.

出版信息

FEBS Lett. 1990 Jun 18;266(1-2):183-6. doi: 10.1016/0014-5793(90)81535-v.

Abstract

The isozyme A of L-2-hydroxyacid oxidase is a peroxisomal flavoenzyme that catalyzes the oxidation of short-chain aliphatic L-2-hydroxyacids in many tissues of higher organisms. A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The N-terminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B.

摘要

L-2-羟酸氧化酶同工酶A是一种过氧化物酶体黄素酶,可催化高等生物许多组织中短链脂肪族L-2-羟酸的氧化。一种新的纯化方法使我们能够从鸡肝中获得纯化了1400倍的该酶。发现多肽链的N端氨基酸与菠菜乙醇酸氧化酶一样被封闭,这与大鼠肾脏同工酶B不同。其氨基酸组成与其他已知的L-2-羟酸氧化酶相当。尽管底物特异性不同,但在鸡肝L-2-羟酸同工酶A和大鼠肾脏同工酶B之间仍观察到一些免疫同源性。

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