从大鼠肝脏胞质溶胶和染色质中分离出的低分子量酸性磷酸酶的特性。
Properties of low-molecular-weight acid phosphatases isolated from cytosol and chromatin of rat liver.
作者信息
Gałka M, Dziembor-Gryszkiewicz E, Kos S, Ostrowski W
出版信息
Acta Biochim Pol. 1980;27(3-4):281-93.
PMID:7269973
Abstract
- Acid phosphatases (orthophosphoric-monoester phosphohydrolases, acid optimum, EC 3.1.3.2) of low molecular weight were isolated from cytosol and chromatin of rat liver cells. The cytosolic enzyme was homogeneous on SDS-polyacrylamide-gel electrophoresis at pH 8.3 (mol. wt. 16 000+/-3000). Both enzymes showed similar electrophoretic mobility and molecular weight but they differed in substrate specificity, response to inhibitors and susceptibility to SH-protecting reagents.
摘要
- 从大鼠肝细胞的胞质溶胶和染色质中分离出了低分子量的酸性磷酸酶（正磷酸单酯磷酸水解酶，最适pH酸性，EC 3.1.3.2）。胞质溶胶酶在pH 8.3的SDS - 聚丙烯酰胺凝胶电泳上呈均一性（分子量16000±3000）。两种酶显示出相似的电泳迁移率和分子量，但它们在底物特异性、对抑制剂的反应以及对SH保护试剂的敏感性方面存在差异。
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