Portal de Periódicos da CAPES

An activity staining method of α-1,4-glucan branching enzyme by the cooperative action with glycogen phosphorylase immobilized within polyacrylamide gels

1980; Elsevier BV; Volume: 108; Issue: 1 Linguagem: Inglês

10.1016/0003-2697(80)90688-0

1096-0309

Kimihiko Satoh, Kiyomi Sato,

Microbial Metabolites in Food Biotechnology

A new sensitive method for the activity staining of α-1,4-glucan branching enzyme on polyacrylamide disc gels has been developed. Rabbit skeletal muscle glycogen phosphorylase b is entrapped within running gels prior to electrophoresis in order to catalyze the cooperative synthesis of glycogen with branching enzyme in the absence of primer glycogen. By the present method, it has been made clear that the primer-independent glycogen synthetic activity of glycogen phosphorylase B′ previously observed in rat tissues (K. Satoh, F. Imai, and K. Sato, 1978, FEBS Lett.95, 239–242) is caused by the combined action of the branching enzyme and reassociated brain-type isozyme of glycogen phosphorylase which is dissociable on electrophoresis.