HORDEUM-VULGARE SEEDLINGS AMINE OXIDASE - PURIFICATION AND PROPERTIES

被引：19

作者：

COGONI, A

PIRAS, C

FARCI, R

MELIS, A

FLORIS, G

机构：

[1] Istituto di Chimica Biologica, Università di Cagliari, 09125 Cagliari, via della Pineta

来源：

PLANT PHYSIOLOGY | 1990年 / 93卷 / 02期

关键词：

D O I：

10.1104/pp.93.2.818

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Although no amine oxidase could be detected in crude extracts, the enzyme has been purified to apparent homogeneity from Hordeum vulgare seedlings using ammonium sulfate precipitation and chromatography on DEAE cellulose, Hydroxylapatite, and Sephadex G200 columns. Gel filtration experiments indicate a molecular weight of about 150,000. The pH optimum of the enzyme was found to be 7.5 in potassium phosphate buffer. The spectrum of ultraviolet and visible regions were similar to Cu-amine oxidase from Leguminosae.

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页码：818 / 821

页数：4

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