Ultracentrifugation studies of purified mouse hepatic catalase revealed that 5-7% of the total material consists of a form with a higher molecular weight than the bulk of the catalase. The two components were separated by sucrose-gradient centrifugation. Polyacrylamide-gel electrophoresis (in borate buffer) demonstrated that high-molecular-weight catalase is enriched in a more slowly migrating component, and sodium dodecyl sulphate/polyacrylamide gel-electrophoresis demonstrated that the molecular weight of the subunits of the high-molecular-weight material is identical with that of the subunits of the major form. These results suggest that high-molecular-weight catalase consists of subunits that are not markedly distinct from those present in the normal catalase tetramer.
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June 1977
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Research Article|
June 01 1977
Presence of a high-molecular-weight form of catalase in enzyme purified from mouse liver Available to Purchase
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1977 London: The Biochemical Society
1977
Biochem J (1977) 163 (3): 449–453.
Citation
M B Baird, H R Massie, L S Birnbaum; Presence of a high-molecular-weight form of catalase in enzyme purified from mouse liver. Biochem J 1 June 1977; 163 (3): 449–453. doi: https://doi.org/10.1042/bj1630449
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