Primary structure of the activation segment of procarboxypeptidase A from porcine pancreas.
The complete primary structure of the activation segment of monomeric procarboxypeptidase A from porcine pancreas has been determined by automated and manual Edman-like degradation methods performed on its fragments generated by enzymatic cleavage. The polypeptide consists of 94 residues, with a molecular mass of 10,768, and presents a high proportion of acidic and hydrophobic residues and a proline-rich region in the center of the molecule. Comparison of this sequence with the already reported equivalent sequence deduced from rat procarboxypeptidase A cDNA reveals a very high degree of homology between the two propeptides (up to a 81% of identities), which is even higher in certain large zones of the molecule.
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D002851:Chromatography, High Pressure Liquid; D004792:Enzyme Precursors; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010446:Peptide Fragments; D013552:Swine
D004792:Enzyme Precursors; D010446:Peptide Fragments; D002268:Carboxypeptidases; D043422:Carboxypeptidases A