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豌豆(Pisum sativum)二胺氧化酶含有吡咯喹啉醌作为辅因子。

Pea (Pisum sativum) diamine oxidase contains pyrroloquinoline quinone as a cofactor.

作者信息

Glatz Z, Kovár J, Macholán L, Pec P

出版信息

Biochem J. 1987 Mar 1;242(2):603-6. doi: 10.1042/bj2420603.

Abstract

Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of the homogeneous enzyme and also analysed the hydrolysed protein by several methods. The data presented here suggest that the carbonyl cofactor of diamine oxidase is firmly bound pyrroloquinoline quinone.

摘要

通过一种涉及两步高效液相色谱的新纯化程序,从豌豆(Pisum sativum)幼苗中制备了二胺氧化酶。我们研究了该纯酶的光学和电化学性质,并通过多种方法分析了水解蛋白。本文给出的数据表明,二胺氧化酶的羰基辅因子是牢固结合的吡咯喹啉醌。

相似文献

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Primary structure of a pyrroloquinoline quinone (PQQ) containing peptide isolated from porcine kidney diamine oxidase.
Biochem Biophys Res Commun. 1989 Mar 15;159(2):726-33. doi: 10.1016/0006-291x(89)90055-7.

本文引用的文献

1
[Purification and characterization of diamine oxidase from peas].[豌豆中二胺氧化酶的纯化与特性分析]
Hoppe Seylers Z Physiol Chem. 1961 Dec 21;326:200-11. doi: 10.1515/bchm2.1961.326.1.200.
5
Cryoenzymology and spectrophotometry of pea seedling diamine oxidase.
Biochemistry. 1980 Apr 15;19(8):1617-21. doi: 10.1021/bi00549a014.

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