PURIFICATION AND SOME PROPERTIES OF AN AMINE OXIDASE FROM SOYBEAN SEEDLINGS

被引：8
|
作者：
NIKOLOV, I [1 ]
PAVLOV, V [1 ]
MINKOV, I [1 ]
DAMJANOV, D [1 ]
机构：
[1] ACAD MED SOFIA,ONCOL RES INST,BU-1156 SOFIA,BULGARIA
来源：
EXPERIENTIA | 1990年 / 46卷 / 07期
关键词：
amine oxidase; Glycine max; putrescine; soybean seedlings; spermidine; spermine;
D O I：
10.1007/BF01939962
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
An amine oxidase was purified 447-fold from soybean seedlings and some of its properties were investigated. The molecular weight of the enzyme was estimated to be 25,000. It was most active towards putrescine, followed by spermidine and spermine. Km-values for these substrates were relatively close. The enzyme was strongly inhibited by carbonyl reagents, such as semicarbazide and aminoguanidine. © 1990 Birkhäuser Verlag Basel.
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页码：765 / 767
页数：3
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