Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-1-21
pubmed:abstractText
High performance liquid chromatography maps of tryptic and chymotryptic peptides from the W and L forms of rat phenylalanine hydroxylase differed by one peptide. Sequencing of the variant tryptic peptides showed a substitution of threonine in the W form by isoleucine in the L form and this same difference was confirmed in the chymotryptic peptides. This allelic substitution would result from a nucleotide change of ACA to ATA at amino acid position 371 of the full phenylalanine hydroxylase sequence. Altered sodium dodecyl sulphate binding is postulated to explain the change in mobility of the proteins observed on sodium dodecyl sulphate/polyacrylamide gels.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
236
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
679-83
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
The W and L allelic forms of phenylalanine hydroxylase in the rat differ by a threonine to isoleucine substitution.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't