Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-6-23
pubmed:abstractText
Two-dimensional peptide map analysis was used to determine the structural homology among the '100 kDa'-group of polypeptides. There are at least six distinct polypeptides whose apparent molecular weights are 116, 113, 111, 108, 105 and 100 kDa. The molar ratio of the '100 kDa'-group of polypeptides to three clathrin monomers (equivalent to one triskelion) is 1.2:1. There are three families of polypeptides in the '100 kDa'-group as determined by two-dimensional peptide map analysis. They are 116 and 113 kDa polypeptides, 111, 108, and 105 kDa polypeptides and 100 kDa polypeptide. However, all six polypeptides apparently show a series of homologous peptides. It is suggested that the 100-116 kDa polypeptides may bind to triskelions at the area of homology that is found in the 100-116 kDa polypeptides.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
924
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
303-11
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Analysis of 100 kDa polypeptides from coated vesicles of bovine brain: two-dimensional tryptic and chymotryptic maps.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.