Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-5-20
pubmed:databankReference
pubmed:abstractText
Access to the nucleotide sequence of parvalbumin from chicken muscle was gained via the polymerase chain reaction. In the absence of specific amino acid sequence data, the PCR primers were based on consensus data for the two parvalbumin Ca2(+)-binding sites. The 137 bp fragment obtained by amplification clearly codes for a parvalbumin, as judged by the presence of 10 invariant codons within the sequence flanked by the primers. When used to probe poly(A)+ RNA from chicken muscle, the fragment recognizes an 800 nucleotide transcript. The translated nucleotide sequence of the muscle protein is unmistakably distinct from that of the thymus-specific parvalbumin known as avian thymic hormone. Of the 31 amplified residues, the two proteins differ at 14. The presence of a distinct parvalbumin in chicken thymus is consistent with the potent effector role proposed for the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
328-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Avian thymic hormone and chicken (muscle) parvalbumin are distinct proteins: isolation of a muscle parvalbumin cDNA fragment by PCR.
pubmed:affiliation
Department of Chemistry, New Mexico State University, Las Cruces 88003.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.