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Carboxypeptidase inhibitor from potatoes. Interaction with derivatives of carboxypeptidase A
Biochemistry, 1976The mechanism of action of a carboxypeptidase inhibitor from potatoes has been probed by studying its interaction with derivatives of carboxypeptidase A containing modified residues at the active site. Arsanilazocarboxypeptidase A, a derivative containing a chromophore attached to tyrosine 248, exhibits a circular dichroism spectrum which is sensitive ...
H, Ako +3 more
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Biokhimiia (Moscow, Russia), 1984
Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
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Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
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Carboxypeptidase A: A Protein and an Enzyme
1971Publisher Summary This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A (CPA), and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme. In particular, it discusses the basis for substrate specificity, modes of binding, and possible mechanisms of hydrolytic ...
F A, Quiocho, W N, Lipscomb
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