Ivanova N M, Vaganova T I, Strongin A Ia, Stepanov V M
Biokhimiia. 1977 May;42(5):843-9.
Homogenious leucine aminopeptidase is purified from "oryzine"--mixture of enzymes produced by surface culture of Asperigillus oryzae using treatment with activated characoal, followed by DEAE-cellulose and hydroxylapatite chromatographies, Biogel P-100 gel-filtration and polyacrylamide-gel electrophoresis. The enzyme has pH optimum 9.0 and the molecular weight 37500 as estimated by gil-filtration through Sephadex G-100 (superfine) and SDS-polyacrylamide gel electrophoresis. Leucine aminopeptidase from Asp. oryzae has a broad substrate specificity, therefore, cleaving with the highest rate the peptides carrying N-terminal leucine. The enzyme is completely inhibited with EDTA and beta-mercaptoethanol, and it is a metalloenzyme.
从“米曲酶素”（米曲霉表面培养产生的酶混合物）中纯化出均一的亮氨酸氨肽酶，方法是先用活性炭处理，然后进行DEAE - 纤维素和羟基磷灰石层析、Biogel P - 100凝胶过滤以及聚丙烯酰胺凝胶电泳。通过Sephadex G - 100（超细）凝胶过滤和SDS - 聚丙烯酰胺凝胶电泳估计，该酶的最适pH为9.0，分子量为37500。米曲霉的亮氨酸氨肽酶具有广泛的底物特异性，因此，对携带N - 末端亮氨酸的肽切割速率最高。该酶被EDTA和β - 巯基乙醇完全抑制，它是一种金属酶。
