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[Carbonic Anhydrases of Bovine Erythrocytes: Comparative Study of the Anhydrase and Esterase Activity of Different Forms]

[Carbonic Anhydrases of Bovine Erythrocytes: Comparative Study of the Anhydrase and Esterase Activity of Different Forms]

J M Gulian, D Faure, J Buc, M Charrel

Biochimie. 1978 Sep 4;60(5):473-8.

PMID: 100147

Abstract:

Comparative study of esterase activities (p- and o-nitrophenylacetate) allowed to characterize three groups of bovine erythrocyte carbonic anhydrases:--the first one includes CI, CII (isozyme of CI) and CIr ("artificial" product of CI).--the second one includes native CIv1 and "artificial" CIv1, first conformational variants of CI,--finally CIv2, second "artificial" conformational variant of CI. Possible modifications of the enzyme site between the first and the other enzyme groups are discussed. Except CIv2 of lower activity, all the products have identical carbonic anhydrase activity. The catalytic constants Km ap and kcat ap for hydrolysis of p-nitrophenylacetate have been determined for all enzymes; this study confirms the lower activity of CIv2.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001030	Carbonic Anhydrase from bovine erythrocytes		9001-03-0	Price

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