title: The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A.
abstract: The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A subunit I has been determined by automated Edman degradation of the cyanogen bromide fractions derived from the precursor protein. The activation peptide contains 94 amino acid residues in a unique sequence which precedes directly the amino-terminal alanine residue of carboxypeptidase A alpha. A notable feature of the activation peptide is the presence of acidic amino acid residues immediately preceding the site of activation. The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A shows extensive similarity to those of the corresponding porcine and rat enzymes.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle 98195.
authors.forename: R D
authors.initials: RD
authors.lastname: Wade
authors.forename: G M
authors.initials: GM
authors.lastname: Hass
authors.forename: S
authors.initials: S
authors.lastname: Kumar
authors.forename: K A
authors.initials: KA
authors.lastname: Walsh
authors.forename: H
authors.initials: H
authors.lastname: Neurath
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000032:analysis*; D043422:Carboxypeptidases A; D002417:Cattle; D003488:Cyanogen Bromide; D004792:Enzyme Precursors / Q000032:analysis*; D006868:Hydrolysis; D008969:Molecular Sequence Data
chemical_list: D004792:Enzyme Precursors; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D003488:Cyanogen Bromide