抄録
one component of molecular weight 30,000 in the supernatant on 65% ammonium sulfate fractionation of the hemolysate was isolated by the method of Sephadex G-75 and CM-cellulose column chromatography, and electrofocusing.
The physicochemical properties of this protein were as follows; molecular weight 30,000±3,000, isoelectric point pH 6.0. Amino acid analysis was performed. lmmunochemical reaction with arlti human carbonic anhydrase B serum was observed. From the above results, this protein was estimated as carbonic anhydrase A.
