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[人血液有形成分中超氧化物歧化酶分子形式的活性及电泳多样性]

[Activity and electrophoretic multiplicity of molecular forms of superoxide dismutase in the formed elements of human blood].

作者信息

Gusev V A, Lamchingiĭn T, Gerasimov A M

出版信息

Biull Eksp Biol Med. 1977 Aug;84(8):166-8.

PMID:907818
Abstract

When calculated per protein content the level of super-oxide dismutase (SOD) activity in various human blood cells proved to decrease as follows: platelet greater than erythrocyte greater than greater than lymphocyte greater than granulocyte. During gel electrophoresis of granulocyte, lymphocyte and platelet homogenates three zones of SOD activity were revealed. Two enzyme fractions disappearing after the cyanide treatment were found in the erythrocyte lysates after the removal of hemoglobin. Of the two SOD fractions of platelets, lymphocytes, and granulocytes rapidly migrating to the anode, by the capacity to be inhibited with cyanide or organic solvents the first SOD fraction was attributed to cytosol enzyme, while the second one -- to mitochondrial enzyme. The third cathode fraction was not identified. The functional role of SOD in specialized blood cells and the causes of the enzyme heterogeneity are discussed.

摘要

按蛋白质含量计算时,各种人体血细胞中超氧化物歧化酶(SOD)活性水平呈如下降低趋势:血小板>红细胞>>淋巴细胞>粒细胞。在对粒细胞、淋巴细胞和血小板匀浆进行凝胶电泳时,发现了三个SOD活性区。去除血红蛋白后,在红细胞裂解物中发现了两个经氰化物处理后消失的酶组分。在血小板、淋巴细胞和粒细胞中,有两个SOD组分快速向阳极迁移,根据其被氰化物或有机溶剂抑制的能力,第一个SOD组分被归为胞质溶胶酶,而第二个则归为线粒体酶。第三个阴极组分未被鉴定。文中讨论了SOD在特殊血细胞中的功能作用以及酶异质性的原因。

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