Linked Life Data

17516654

Source:http://linkedlifedata.com/resource/pubmed/id/17516654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2007-6-6
pubmed:abstractText
The ability of phaseolin to act as an acyl donor and acceptor substrate of transglutaminase was studied by using an enzyme isolated from Streptoverticillium mobarense. Phaseolin, a trimeric storage protein from Phaseolus vulgaris L., was shown to possess both glutamine and lysine residues reactive for the enzyme. The extent of transglutaminase-catalyzed cross-linking has been studied in function of both incubation time and enzyme concentration. Native- and SDS-PAGE demonstrated that phaseolin is intra- and intermolecularly cross-linked by transglutaminase and gives rise to different polymers as well as to modified forms of the protein having a similar molecular weight but lower Stokes radius if compared to unmodified phaseolin. Cross-linked phaseolin was found to be more resistant to proteolytic cleavage than the unmodified counterpart, as demonstrated by in vitro trypsin and pepsin digestion experiments. This behavior could suggest novel possible uses of the transglutaminase-modified phaseolin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4717-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris.
pubmed:affiliation
Department of Food Science and School of Biotechnological Sciences, University of Naples Federico II, Parco Gussone, 80055 Portici, Naples, Italy. loredana.mariniello@unina.it
pubmed:publicationType
Journal Article