Properties of catalase subfractions separated by chromatofocusing of acatalasemia hemolysates

Acta Medica Okayama
M Ogata, J Mizugaki

Abstract

Erythrocyte catalase in normal and Japanese type acatalasemia hemolysates was separated by chromatofocusing into several fractions in the pH range of 6.1 to 5.7. Normal hemolysate gave a major peak of catalase activity with a pH of 6.1 to 5.5, while acatalasemia hemolysate gave several small peaks in this pH range and a main peak with a pH of 6.6 to 6.2. The main protein band in catalase active fractions separated from normal erythrocytes had a molecular weight of 60,000 by SDS polyacrylamide gel electrophoresis. A similar faint protein band having a molecular weight of 60,000 was also found in acatalasemia hemolysate in addition to a fairly intense band with a molecular weight of about 30,000. Catalase active fractions from normal erythrocytes reacted with antihuman erythrocyte catalase rabbit serum by double immunodiffusion.

Related Concepts

Catalase T
SDS-PAGE
Erythrocytes
Hemolysis
Isoelectric Focusing
Acatalasemia Swiss Type

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