Abstract
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.
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