Linked Life Data

7436050

Source:http://linkedlifedata.com/resource/pubmed/id/7436050

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-1-16
pubmed:abstractText
A comparison is made of the four main components of an homozygous variant (A or D2D2) of bovine serum transferrin. These are designated I-IV in order of increasing mobility in electrophoresis at pH 7.5. Components I, II, III and IV have 2,2,3 and 3 residues of sialic acid per transferrin molecule and appear to correspond to components 2a, 2b, 3a and 3b respectively of Stratil & Spooner (1971). The difference between components I and II and between III and IV does not reside in sialic acid differences. On the basis of peptide maps of reduced carboxamidomethylated components, urea-starch gel electrophoresis and quantitative sequence studies, it is concluded that components II and IV have a scission in the peptide chain. By homology with the sequency of MacGillivray et al. (1977) for human serum transferrin it is suggested that the scission occurs between residues 55 and 54 from the C-terminus and this portion of the chain has a 'molecular' weight of ca. 6000. The implications are briefly discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-3480
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-75
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Nature of the heterogeneity within genetic variants of bovine serum transferrin.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't