Studies on Peroxisomes

VIII. Evidence for Framework Protein of the Cores of Rat Liver Peroxisomes

Abstract

The cores of peroxisomes were purified 670 fold from a rat liver homogenate and the protein in the preparation was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
Two bands of protein were detected on 10% polyacrylamide gel, and their molecular weights were calculated to be about 32, 000 and 27, 000.
On treatment of the core fraction with alkali, urate oxidase was solubilized and on 10% polyacrylamide gel this fraction gave a single band of protein with an estimated molecular weight of 32, 000.
These results suggests that the protein component having a molecular weight of 27, 000 is the framework protein of the core of rat liver peroxisomes.