Key result
Carboxypeptidase P, purified from swine kidney microsomes, has a molecular weight of 240,000, a pH optimum of 7.75, and preferentially cleaves substrates with a penultimate prolyl residue.
Population
Swine kidney microsomes
Design
Preclinical
Authors
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Animal enzyme data warrant no clinical use; leaves open human peptide metabolism studies.
The study identifies and characterizes carboxypeptidase P from swine kidney, an enzyme that preferentially cleaves peptides with a penultimate proline residue.
Dehm et al. (1970) studied this question. Enzyme purification and characterization was evaluated on Enzyme characteristics (molecular weight, pH optimum, substrate specificity). Carboxypeptidase P, purified from swine kidney microsomes, has a molecular weight of 240,000, a pH optimum of 7.75, and preferentially cleaves substrates with a penultimate prolyl residue.
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