title: Hydroxylamine-stable covalent linkage of myristic acid in G0 alpha, a guanine nucleotide-binding protein of bovine brain.
abstract: G0 alpha, a guanine nucleotide-binding protein with a strong homology to the G1 alpha and Gs alpha regulatory proteins of adenylate cyclase, is shown to contain myristic acid. The attachment of myristate to the protein is stable to hydroxylamine treatment, and since the amino-terminal sequence of G0 alpha is typical of proteins with amino-terminal myristate, the inference is strong that G0 alpha is also myristylated at its amino-terminal glycine.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism*; D002417:Cattle; D019204:GTP-Binding Proteins / Q000378:metabolism*; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology*; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D006898:Hydroxylamines; D009227:Myristic Acids; D019814:Myristic Acid; D019811:Hydroxylamine; D019204:GTP-Binding Proteins