On the interactions of catalase with subcellular structure

✍ Scribed by Michael Pegg; Denis Crane; Colin Masters

• Book ID: 104674678
• Publisher: Springer
• Year: 1989
• Tongue: English
• Weight: 649 KB
• Volume: 86
• Category: Article
• ISSN: 0300-8177
• DOI: 10.1007/bf00231692

✦ Synopsis

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.