Verbilenko S V, Kolodzeiskaia M V
Ukr Biokhim Zh (1978). 1980 May-Jun;52(3):329-34.
The paper deals with properties of Aspergillus oryzae (strain KC) purified aminopeptidase. The enzyme is homogeneous in electrophoresis in polyacrylamide gel and enzyme-electrophoresis with the synthetic substrate leucyl-beta-naphthylamide applied. The molecular mass is 60000-61000 Daltons. The amino acidic composition of the enzyme is characterized by a high content of dicarboxylic acids. The substrate specificity is studied. Leucyl-glycyl-glycin and leucinamide are most intensive in splitting. Peptides with a blocked amino group are not hydrolyzed.
本文研究了米曲霉（菌株KC）纯化的氨肽酶的性质。该酶在聚丙烯酰胺凝胶电泳以及使用合成底物亮氨酰-β-萘酰胺的酶电泳中均表现为均一。分子量为60000 - 61000道尔顿。该酶的氨基酸组成特点是二羧酸含量高。对其底物特异性进行了研究。亮氨酰-甘氨酰-甘氨酸和亮氨酰胺的裂解作用最强。氨基被封闭的肽不被水解。
