Linked Life Data

8108494

Source:http://linkedlifedata.com/resource/pubmed/id/8108494

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-23
pubmed:databankReference
pubmed:abstractText
A polygalacturonase inhibitor glycoprotein with an apparent molecular mass of 43 kD was purified from pear (Pyrus communis L. cv Bartlett) fruit. Chemical deglycosylation of this protein decreased the molecular mass to 34 kD. Gas chromatographic analysis suggests that N-linked glycosylation accounts for the majority of sugar moieties. Partial amino acid sequence analysis of the purified polygalacturonase inhibitor protein provided information used to amplify a corresponding cDNA by polymerase chain reactions. Multiple cloned products of these reactions were sequenced and the same open reading frame was identified in all of the products. It encodes a 36.5-kD polypeptide containing the amino acid sequences determined by protein sequencing and predicts a putative signal sequence of 24 amino acids and seven potential N-glycosylation sites. The expression of polygalacturonase inhibitor is regulated in a tissue-specific manner. Activity and mRNA level were much higher in fruit than in flowers or leaves.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
102
pubmed:geneSymbol
PGIP
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-8
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Molecular characterization of a polygalacturonase inhibitor from Pyrus communis L. cv Bartlett.
pubmed:affiliation
Department of Pomology, University of California, Davis 95616.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't