期刊名称：Studia Universitatis Moldaviae: Stiinte Exacte si Economice
印刷版ISSN：1857-2073
电子版ISSN：2345-1033
出版年度：2007
期号：7(07)
页码：133-138
出版社：Moldova State University
摘要：Proteinase A, that possibly participate in the degradation of phaseolin, the main 7S storage protein of kidney bean(Phaseolus vulgaris L.), was isolated as a 35-kDa polypeptide from germinating kidney bean seeds and partially characterised.According to its properties it belong to a group of homologous cysteine proteinases of the papain family thatparticipate in storage protein mobilisation during seeds geminating of many plants. The proteinases of this group hydrolizestorage proteins to short peptides. Dispite close similarity to proteinase A from vetch, proteinase A from kidney beanhydrolyse phaseolin by non-co-operative mechanism. This action is limited to the cleavage of subunits into two approximatelyequal parts and to spliting off a number of short peptides which result in the modification of quaternary structure ofphaseolin molecule. It is similar to the action on phaseolin of other proteases, both endogenous and exogenous, andprovide another example of the importance of phaseolin structure in the explanation of its resistance to proteolysis
