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ID 30710
JaLCDOI
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Author
Ogata, Masana
Mizugaki, Junko
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.

Keywords
acatalasemia
SDS polyacrylamide gel electrophoresis
Amo Type
Article
Publication Title
Acta Medica Okayama
Published Date
1982-02
Volume
volume36
Issue
issue1
Publisher
Okayama University Medical School
Start Page
73
End Page
76
ISSN
0386-300X
NCID
AA00508441
Content Type
Journal Article
language
English
File Version
publisher
Refereed
True
PubMed ID
Web of Science KeyUT