A different structural feature for carbonic anhydrases in human erythrocytes.
This study presents a different structural feature for carbonic anhydrase in human erythrocytes. Carbonic anhydrase isozymes (CA-I and CA-II) were purified from an erythrocyte pool of 20 healthy subjects. For purification, Sepharose-4B-L-tyrosine-sulfanilamide affinity column was used. Resnets from 3-10% discontinuous SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed a single band for CA-I and two distinct bands 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 different value. Native electrophoresis showed two bands for CA-I, and it showed three bands for CA-II. It can be concluded that CA-I is a polymer composed of a single promoter and CA-II has three different polymers composed of two distinct promoters, suggesting a new structural feature of human erythrocyte carbonic anhydrase isozymes.
Demir
N
N
Atatürk Universty Science and Art Faculty Chemistry Department, Erzurum Turkiye.
Demir
Y
Y
Bakan
E
E
Küfrevioğlu
O I
OI
D002256:Carbonic Anhydrases / Q000097:blood* / Q000737:chemistry* / Q000302:isolation & purification; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D004950:Esterases / Q000097:blood; D006801:Humans; D007527:Isoenzymes / Q000097:blood* / Q000737:chemistry* / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight
D007527:Isoenzymes; D004950:Esterases; D002256:Carbonic Anhydrases