期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 8, 页码 2388-2389出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja0778038
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资金
- NIGMS NIH HHS [GM063740] Funding Source: Medline
Oxidation of active site residues (His and Trp), following catalytic inactivation of human carbonic anhydrase I by a copper-ATCUN conjugate of sulfanilimide, is evidenced by mass spectrometric analysis of tryptic and chymotryptic digest of the modified CA-I. Accordingly, residue oxidation rather than protein cleavage is the demonstrated mods of inactivation. An apparent second-order rate constant, k(2) similar to 7600 M(-1)min(-1), has been determined for catalytic inactivation of CA-I.
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