Molecular and catalytic properties of rabbit testicular dipeptidyl carboxypeptidase.
Rabbit testicular dipeptidyl carboxypeptidase activity was purified by a procedure exploiting its affinity for N-alpha-[1-(S)-carboxy-3-phenylpropyl]-L-lysyl-L-proline. The molecular, catalytic, and immunological properties of the testicular enzyme are presented and compared with the corresponding properties of pulmonary angiotensin-converting enzyme. Although catalytically similar and immunologically related to pulmonary dipeptidyl carboxypeptidase, the testicular enzyme has a molecular weight (100,000) which is lower by a factor of about one-third and differs in its NH2 and COOH termini. Furthermore, we present evidence that the testicular enzyme is not a post-translation product of the pulmonary type enzyme. These data suggest that testicular and pulmonary dipeptidyl carboxypeptidase are two distinct proteins which are catalytically similar and immunologically closely related.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D002241:Carbohydrates / Q000032:analysis; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D011817:Rabbits; D011863:Radioimmunoassay; D013737:Testis / Q000201:enzymology*
D000596:Amino Acids; D000906:Antibodies; D000936:Antigen-Antibody Complex; D002241:Carbohydrates; D010450:Endopeptidases; C020071:dipeptidyl carboxypeptidase