米曲霉中两种膜酸性蛋白酶分子形式的细胞内定位

Intracellular localization of two molecular forms of membrane acid protease in Aspergillus oryzae.

作者信息

Tsujita Y, Endo A

出版信息

J Biochem. 1980 Jul;88(1):113-20.

Abstract

The intracellular localization of two forms of membrane-bound acid protease (M1 and M2) [EC 3.4.23.6] of Aspergillus oryzae (Tsujita, Y. & Endo, A. (1978) Eur. J. Biochem. 84, 347-353) was investigated. When the mycelia were treated with wall-lytic enzymes, M2 remained in the cells but most of M2 was solubilized and released. The cell wall fraction obtained by mechanical disruption of the mycelia contained less than 5% of the total acid protease activity in the cells. Subcellular fractionation of the membranes obtained from burst spheroplasts showed that the acid protease was present in both rough and smooth microsomes. Acid protease M1 was predominant in the former and M2 in the latter, possibly on the surface of the cytoplasmic membranes.

摘要

对米曲霉的两种形式的膜结合酸性蛋白酶（M1和M2）[EC 3.4.23.6]的细胞内定位进行了研究（辻田义、远藤安（1978年），《欧洲生物化学杂志》84卷，347 - 353页）。当用细胞壁溶解酶处理菌丝体时，M2保留在细胞内，但大部分M2被溶解并释放出来。通过机械破碎菌丝体获得的细胞壁部分所含的酸性蛋白酶活性不到细胞中总酸性蛋白酶活性的5%。对从破裂的原生质体获得的膜进行亚细胞分级分离表明，酸性蛋白酶存在于粗面和滑面微粒体中。酸性蛋白酶M1在前者中占主导，M2在后者中占主导，可能位于细胞质膜表面。