Protease susceptibility of zinc- and apo-carboxypeptidase A.
Proteases in preparations of carboxypeptidase A progressively inactivate solutions of the apoenzyme but not the metal-containing enzyme. Free amino acids generated by proteolysis interfere with spectral studies after reconstituting the apoenzyme with cobalt. Purification by affinity chromatography eliminates this effect. Affinity-purified apoenzyme is susceptible to digestion with chymotrypsin but the metalloenzyme is not.
D001051:Apoenzymes / Q000378:metabolism*; D001059:Apoproteins / Q000378:metabolism*; D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D003460:Crystallization; D010447:Peptide Hydrolases / Q000378:metabolism*; D012996:Solutions; D013053:Spectrophotometry; D015032:Zinc
D001051:Apoenzymes; D001059:Apoproteins; D012996:Solutions; D002268:Carboxypeptidases; D010447:Peptide Hydrolases; D043422:Carboxypeptidases A; D015032:Zinc