红细胞中的一种高分子量肽水解酶。

A high molecular weight peptide hydrolase in erythrocytes.

Edmunds T, Pennington R J

Int J Biochem. 1982;14(8):701-3. doi: 10.1016/0020-711x(82)90005-2.

Abstract

A peptide hydrolase has been partially purified from the soluble fraction of erythrocyte lysates. 2. The enzyme has a molecular weight of approximately 600,000 and hydrolyses the chymotrypsin substrate glutaryl-Gly-Gly-Phe-7-amido-4-methylcoumarin (pH optimum 7.0) and the trypsin substrate CBZ-Gly-Gly-Arg-2-naphthylamide. The two activities could not be separated by the purification procedure used. 3. The activity towards glutaryl-Gly-Gly-Phe-7-amido-4-methylcoumarin in rat reticulocytes was four times that in mature erythrocytes. 4. Activity was abolished by 10 microM p-hydroxymercuriphenylsulphonic acid.

摘要

已从红细胞裂解物的可溶性部分中部分纯化出一种肽水解酶。2. 该酶的分子量约为600,000，可水解胰凝乳蛋白酶底物戊二酰 - 甘氨酰 - 苯丙氨酰 - 7 - 氨基 - 4 - 甲基香豆素（最适pH 7.0）和胰蛋白酶底物苄氧羰基 - 甘氨酰 - 甘氨酰 - 精氨酰 - 2 - 萘酰胺。在所采用的纯化过程中，这两种活性无法分离。3. 大鼠网织红细胞中对戊二酰 - 甘氨酰 - 苯丙氨酰 - 7 - 氨基 - 4 - 甲基香豆素的活性是成熟红细胞中的四倍。4. 10微摩尔对羟基汞苯磺酸可使活性丧失。