N. Demir et al., A DIFFERENT STRUCTURAL FEATURE FOR CARBONIC-ANHYDRASES IN HUMAN ERYTHROCYTES, Preparative biochemistry & biotechnology, 27(4), 1997, pp. 279-287
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.