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.
Division of Science and Technology, Griffith University, Brisbane, Australia.
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Pegg
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Crane
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Masters
D000818:Animals; D002374:Catalase / Q000302:isolation & purification / Q000378:metabolism*; D002458:Cell Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000201:enzymology*; D051379:Mice; D008862:Microsomes, Liver / Q000201:enzymology*; D008954:Models, Biological; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000378:metabolism; D009994:Osmolar Concentration; D011485:Protein Binding; D012794:Sialic Acids / Q000378:metabolism
D012794:Sialic Acids; D002374:Catalase; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid