PMID: 6406136Jan 1, 1983Paper

Characterization of a high activity carbonic anhydrase isozyme purified from erythrocytes of Salmo gairdneri

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
G E Hall, R Schraer

Abstract

1. A single, high specific activity carbonic anhydrase (CA) isozyme was present in erythrocytes of the teleostean species Salmo gairdneri (rainbow trout). 2. Purification of trout CA to homogeneity was accomplished using chloroform ethanol extraction, Sephadex G-75 gel filtration, and DEAE Bio-Gel anion exchange chromatography. 3. Trout CA was a zinc metalloenzyme of mol. wt 28,300 and pI9.3. 4. Amino acid analysis indicated the presence of 6 half-cystine residues per enzyme molecule, and the presence of a sulfhydryl reducing agent was required to maintain full activity in vitro. 5. Sulfhydryl modification with both N-ethylmaleimide and acrylonitrile indicated the presence of 3 reactive sulfhydryl groups per CA molecule. Modification of those groups had no direct effect on enzyme activity, but modified CA was no longer subject to inactivation by oxidizing conditions.

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Citations

Feb 22, 2008·Biological Trace Element Research·Hakan SoyutOlcay Hisar
Jan 1, 1984·Comparative Biochemistry and Physiology. A, Comparative Physiology·R Zbanyszek, L S Smith
Jan 1, 1983·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J S KimR Schraer
Sep 27, 2003·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·B L TuftsS G Lund
Jan 15, 2004·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·Hidekazu TohseYasuo Mugiya
Mar 15, 2015·Environmental Toxicology and Pharmacology·Elif Duygu KayaŞükrü Beydemir
Sep 29, 2011·Toxicology and Industrial Health·Hakan Söyüt, Sükrü Beydemir

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