牛主动脉胺氧化酶纯化物的分离纯化程序及其赖氨酰氧化酶活性研究。

A purification procedure for the isolation of homogeneous preparations of bovine aorta amine oxidase and a study of its lysyl oxidase activity.

作者信息

Shieh J J, Tamaye R, Yasunobu K T

出版信息

Biochim Biophys Acta. 1975 Feb 19;377(2):229-38. doi: 10.1016/0005-2744(75)90305-8.

Abstract

It has been reported that bovine aorta amine oxidase oxidizes lysine residues in tropoelastin to allysine (Rucker, R.B. and O'Dell, B.L. (1971) Biochim. Biophys. Acta 235, 32-43). Pure bovine aorta amine oxidase was isolate by DEAE-cellulose, hydroxylapatite, Bio-Gel A-1.5 m and concanavalin A-Sepharose 4B chromatography. Enzymatic, chromatographic and immunochemical tests disclosed that pure bovine aorta amine oxidase was not a lysyl oxidase capable of oxidizing the lysine residues of tropoelastin to allysine; The bovine aorta amine oxidase preparation used by Rucker and O'Dell appears to have been contaminated with lysyl oxidase which is the emzyme that oxidizes some of the lysine residues in tropoelastin and tropocollagen to allysine.

摘要

据报道，牛主动脉胺氧化酶可将原弹性蛋白中的赖氨酸残基氧化为烯赖氨酸（鲁克，R.B. 和奥德尔，B.L.（1971年）《生物化学与生物物理学学报》235卷，第32 - 43页）。通过DEAE - 纤维素、羟基磷灰石、Bio - Gel A - 1.5m和伴刀豆球蛋白A - 琼脂糖4B柱色谱法分离出了纯牛主动脉胺氧化酶。酶学、色谱分析和免疫化学测试表明，纯牛主动脉胺氧化酶并非能够将原弹性蛋白的赖氨酸残基氧化为烯赖氨酸的赖氨酰氧化酶；鲁克和奥德尔所使用的牛主动脉胺氧化酶制剂似乎已被赖氨酰氧化酶污染，赖氨酰氧化酶是一种可将原弹性蛋白和原胶原中的一些赖氨酸残基氧化为烯赖氨酸的酶。