On the interactions of catalase with subcellular structure
Copyright policy )On the interactions of catalase with subcellular structure
The interaction of mouse liver catalase with subcellular membranes was studied, and an ionic interaction with a variety of membranes, including those derived from the microsomes, was observed. The interaction with microsomal membranes was found to be abolished by pre-treatment of catalase with neuraminidase, indicating a functional significance for catalase-bound sialic acid. Catalase activity was found to be enhanced when bound to membranes, and evidence for a weak association of catalase with peroxisomal structure in mouse liver was also obtained. It is concluded that mouse liver catalase has a capacity to bind to a variety of subcellular membranes in vivo and that this interaction may be consistent with a general protective role for the enzyme, as well as being compatible with a model of peroxisomal biogenesis which involves the interaction of catalase with microsomal membranes.
- Griffith University Australia
Osmolar Concentration, Neuraminidase, Intracellular Membranes, Hydrogen-Ion Concentration, Catalase, Cell Fractionation, Models, Biological, N-Acetylneuraminic Acid, Mice, Microsomes, Liver, Sialic Acids, Animals, Electrophoresis, Polyacrylamide Gel, Female, Protein Binding
Osmolar Concentration, Neuraminidase, Intracellular Membranes, Hydrogen-Ion Concentration, Catalase, Cell Fractionation, Models, Biological, N-Acetylneuraminic Acid, Mice, Microsomes, Liver, Sialic Acids, Animals, Electrophoresis, Polyacrylamide Gel, Female, Protein Binding
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