[Purification and partial characterization of the proteinase A from germinated kidney beans [Phaseolus vulgaris]
2007
Rotari, V.
The proteinase A, that possibly participates in the degradation of phaseolin - the main 7S storage protein of kidney bean (Phaseolus vulgaris), was isolated as a 35-kDa polypeptide from germinating kidhey seeds and partially characterized. According to its properties it belongs to a group of homologous cysteine proteinases of the papain family that participate in storage protein mobilisation during seed germinating of many plants. The proteinases of this group hydrolyze storage proteins to short peptides. Despite its close similarity to the proteinase A from vetch, the proteinase A from kidney bean hydrolyzes phaseolin by non-co-operative mechanism. This action is limited to the cleavage of subunits into two approximately equal parts and to splitting off a number of short peptides which result in the modification of quaternary stucture of phaseolin molecule. It is similar to the action on phaseolin of other proteases, both endogenous and exogenous, and provide another example of the importance of phaseolin structure in the explanation of its resistance to proteolysis.
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