Cobalt (3) carboxypeptidase A: preparation and esterase activity |
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| Authors: | E P Kang C B Storm F W Carson |
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| Affiliation: | Department of Chemistry, Howard University Washington, D. C. 20001 USA; Department of Chemistry, American University Washington, D. C. 20016 USA |
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| Abstract: | Co(II) carboxypeptidase A has been oxidized to Co(III) carboxypeptidase A with hydrogen peroxide. The resultant metalloprotein has an absorption spectrum different from that of the Co(II) enzyme and the metal is no longer removable by dialysis. The Co(III) carboxypeptidase A retains esterase activity comparable to that of the Co(II) enzyme and has very low peptidase activity. This demonstrates that scission of a bond to the first coordination sphere of the metal is not necessary for the hydrolysis of ester substrates. |
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