Literature DB >> 18459789

Calcium ions make phytohemagglutinin resistant to trypsin proteolysis.

Diana Morari1, Tatiana Stepurina, Vitalie I Rotari.   

Abstract

To investigate the mechanism of phytohemagglutinin (PHA) susceptibility or resistance to the action of proteolytic enzymes, its in vitro proteolysis by trypsin was studied. It was found that Ca (2+) gives resistance to the native PHA molecule to trypsin proteolysis. In the absence of Ca (2+) trypsin performs a thorough hydrolysis of PHA. At the first stage of trypsin hydrolysis of PHA the formation of a relatively stable high molecular mass product occurs (PHA-T) as a result of non-co-operative proteolysis. At the second stage, the degradation of PHA-T occurs, and this degradation is performed by parallel co-operative proteolysis. This type of proteolysis differs from the action of trypsin on phaseolin, the main storage protein from common bean ( Phaseolus vulgaris L.). The implications of Ca (2+)influence of PHA hydrolysis by trypsin are discussed.

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Year:  2008        PMID: 18459789     DOI: 10.1021/jf0734222

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  3 in total

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Journal:  ACS Sens       Date:  2016-03-24       Impact factor: 7.711

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3.  Two-Step Isolation, Purification, and Characterization of Lectin from Zihua Snap Bean (Phaseolus vulgaris) Seeds.

Authors:  Bin Jiang; Xiaojing Wang; Linlin Wang; Xiaomeng Lv; Dongmei Li; Chunhong Liu; Zhibiao Feng
Journal:  Polymers (Basel)       Date:  2019-05-02       Impact factor: 4.329

  3 in total

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