Holzer H, Bünning P, Meussdoerffer F
Adv Exp Med Biol. 1977;95:271-89. doi: 10.1007/978-1-4757-0719-9_16.
A purification and some properties of proteinase A from yeast are described. A specific macromolecular inhibitor of proteinase A from yeast cytosol has been isolated and shown to be a protein (molecular weight 7,700) consisting of a majority of polar amino acids. Proline, arginine, cysteine and tryptophan were not detected in the inhibitor. Possible biological functions of proteinase A and the proteinase A-inhibitor (and of other yeast proteinases and their inhibitors) in the following processes are discussed: general protein turnover, catabolite inactivation of enzymes, enzyme degradation at starvation and at transition to spore formation, and activation of pre-enzymes and precursor proteins by limited proteolysis.
本文描述了从酵母中纯化蛋白酶A及其一些性质。已从酵母细胞质中分离出一种蛋白酶A的特异性大分子抑制剂，并证明它是一种蛋白质（分子量7700），由大多数极性氨基酸组成。在该抑制剂中未检测到脯氨酸、精氨酸、半胱氨酸和色氨酸。文中讨论了蛋白酶A和蛋白酶A抑制剂（以及其他酵母蛋白酶及其抑制剂）在以下过程中可能的生物学功能：一般蛋白质周转、酶的分解代谢失活、饥饿和向孢子形成转变时酶的降解，以及通过有限的蛋白水解激活前体酶和前体蛋白。
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