| Literature DB >> 7107641 |
J M Wilson, G E Tarr, W C Mahoney, W N Kelley.
Abstract
The entire amino acid sequence of hypoxanthine-guanine phosphoribosyltransferase from human erythrocytes has been defined. Peptide fragments formed by cleavage at arginine, glutamic acid, and methionine residues were analyzed by Edman degradation or digestion with carboxypeptidase. The complete primary structure of human hypoxanthine-guanine phosphoribosyltransferase was established by sequence analysis of 17 peptide fragments, 15 of which were purified by reverse-phase high pressure liquid chromatography. The enzyme is 217 residues long with a molecular weight equal to 24,470. Mass spectroscopy indicated that the NH2-terminal alanine is acetylated.Entities:
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Year: 1982 PMID: 7107641
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157