New forms of bovine carboxypeptidase B and their homologous relationships to carboxypeptidase A.
Two new forms of carboxypeptidase B have been isolated from spontaneously activated bovine pancreatic juice. The fully active enzymes contain an internal split at residues 92-93 and 95-96, respectively. Sequenator analysis of the amino terminal segments of the two chains of the enzyme has extended the sequence information by 51 amino acid residues. Comparison of 125 residues strengthens the hypothesis that carboxypeptidases A and B are homologous both in amino acid sequence and in three-dimensional conformation and implicates Asp-255 as the anionic site of substrate binding of the B enzyme.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002268:Carboxypeptidases / Q000302:isolation & purification*; D002417:Cattle; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D004586:Electrophoresis; D008961:Models, Structural; D010189:Pancreatic Juice / Q000201:enzymology; D011487:Protein Conformation
D002268:Carboxypeptidases