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Aggregationsformen der Rinderleberkatalase
Author(s) -
Diezel W.,
Liebe St.,
Kopperschläger G.,
Hofmann E.
Publication year - 1970
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(70)80048-5
Subject(s) - catalase , differential centrifugation , electrophoresis , chemistry , gel electrophoresis of proteins , density gradient , polyacrylamide gel electrophoresis , molecular mass , gel electrophoresis , centrifugation , chromatography , enzyme , biochemistry , physics , quantum mechanics
Bovine liver catalase is separated into several distinct bands by electrophoresis in a linear concentration gradient of polyacrylamide. Apparently, disc electrophoresis under these conditions leads to a series of enzymatic active forms of catalase. Their molecular weights are: 248,000; 295,000; 368,000; 486,000; 705,000 respectively. Density gradient centrifugation separates catalase into two components with molecular weights of 252,000 and 316,000. The observed differences in molecular weight distribution between gel‐electrophoresis and density gradient centrifugation are discussed.