A DIFFERENT STRUCTURAL FEATURE FOR CARBONIC-ANHYDRASES IN HUMAN ERYTHROCYTES

Citation
N. Demir et al., A DIFFERENT STRUCTURAL FEATURE FOR CARBONIC-ANHYDRASES IN HUMAN ERYTHROCYTES, Preparative biochemistry & biotechnology, 27(4), 1997, pp. 279-287
Citations number
17
ISSN journal
10826068
Volume
27
Issue
4
Year of publication
1997
Pages
279 - 287
Database
ISI
SICI code
1082-6068(1997)27:4<279:ADSFFC>2.0.ZU;2-M
Abstract
This study presents a different structural feature for carbonic anhydr ase in human erythrocytes Carbonic anhydrase isozymes (CA-I and CA-II) were purified from an erythrocyte pool of 20 healthy subjects. For pu rification, Sepharose-4B-L-tyrosine-sulfanilamide affinity column was used. Resnets from 3-10 % discontinuous SDS-polyacrylamide gel electro phoresis (SDS-PAGE) showed a single band for CA-I and two distinct ban ds for CA-II. The molecular weights of the two bands were similar. One peak for CA-I and two peaks for CA-II were obtained in gel filtration . The enzymatic activities of the bands in question were also of diffe rent value. Native electrophoresis showed two bands for CA-I, and it s howed three bands for CA-Tr. It can be concluded that CA-I is a polyme r composed of a single promoter and CA-II has three different polymers composed of two distinct promoters, suggesting a new structural featu re of human erythrocyte carbonic anhydrase isozymes.