ISOLATION AND PROPERTIES OF SUPEROXIDE-DISMUTASE FROM HUMAN BLOOD-PLASMA

被引：0

作者：

DUBININA, EE ^{[1
]}

TURKIN, VV ^{[1
]}

BABENKO, GA ^{[1
]}

ISAKOV, VA ^{[1
]}

机构：

[1] SM KIROV STATE INST ADV MED TRAINING, ST PETERSBURG, RUSSIA

来源：

BIOCHEMISTRY-MOSCOW | 1992年 / 57卷 / 12期

关键词：

SUPEROXIDE DISMUTASE; PLASMA; ANTIOXIDANTS; GEL FILTRATION; PURIFICATION;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A procedure was developed for isolation of superoxide dismutase (SOD) from human blood plasma using gel filtration on Ultrogels AcA-34 and AcA-44 (LKB, Sweden). The purified enzyme appears to be a glycoprotein. It is resistant to heating up to 75-80-degrees-C. Its molecular weight estimated by gel filtration is approximately 147 kD. Comparative analysis of the ability of compounds forming complexes with metals of the enzyme active center was performed to evaluate their inhibitory effects on plasma and erythrocyte SODs. The purified enzyme was shown to differ from Cu,Zn-SOD and to belong to a new type of SOD (extracellular SOD) found in some biological fluids.

引用

页码：1316 / 1323

页数：8

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