Linked Life Data

15333645

Source:http://linkedlifedata.com/resource/pubmed/id/15333645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
406
pubmed:dateCreated
2004-9-21
pubmed:abstractText
Two types of cysteine proteases, low-specificity enzymes from the papain family and Asn-specific from the legumain family are generally considered to be the major endopeptidases responsible for the degradation of seed storage proteins during early seedling growth. The action of the corresponding enzymes (CPPh1 and LLP, respectively) from common bean (Phaseolus vulgaris L.) on phaseolin (the common bean storage protein), and on the homologous soybean (Glycine max (L.) Merrill) storage protein, beta-conglycinin, was studied. Under the action of LLP, proteolysis of phaseolin was limited to cleavage of its interdomain linker. No cleavage of the interdomain linker occurred in beta-conglycinin with LLP. LLP action was restricted to splitting off the disordered N-terminal extensions of alpha and alpha' subunits. No extensive hydrolysis (degradation to short TCA-soluble peptides) of either protein occurred under the action of LLP. CPPh1 cleaved the phaseolin subunits into roughly half-sized fragments at the onset of proteolysis. The cleavage was accompanied by a small (8-10%) decrease of protein. No decrease of protein occurred with further incubation. Thus the two most active proteinases detected in common bean seedlings individually were incapable of the extensive degradation of phaseolin. Extensive hydrolysis of phaseolin was only achieved by the consecutive action of LLP and CPPh1. Similar cleavages occurred during the action of CPPh1 on beta-conglycinin. However, by contrast with phaseolin, CPPh1 by itself accomplished the extensive hydrolysis of beta-conglycinin. The differences in the course of proteolysis of the proteins studied were determined by their structural peculiarities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-0957
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2241-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins.
pubmed:affiliation
Laboratory of Protein Chemistry, Moldova State University, Mateevici str.60, MD-2009, Kishinev, Republic of Moldov.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't