An electron microscopic and enzymic study of rat liver peroxisomal nucleoid core and its association with urate oxidase.
The appearance of the characteristic crystalloid core of rat liver peroxisomes is emulated by the electron microscopic (EM) appearance of highly purified urate oxidase prepared from the same tissue. The purity of the enzyme preparation was established by gel electrophoresis under various conditions and the specific enzyme activity was at least as high as any previously reported. The amino acid composition of urate oxidase was determined. As additional evidence for close association of the peroxisomal core with urate oxidase, it was demonstrated that the biphasic changes in rat liver urate oxidase activity in response to prolonged starvation were paralleled by changes in the EM appearance of peroxisomes. Under comparable conditions catalase, another peroxisomal enzyme, did not show the same changes in activity as did urate oxidase. Evidence for the possible identity of urate oxidase with the peroxisomal crystalloid of rat liver has been presented, all materials having been obtained from, and experiments performed with, the rat.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005260:Female; D006651:Histocytochemistry; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D008297:Male; D008830:Microbodies / Q000032:analysis / Q000201:enzymology* / Q000648:ultrastructure; D008970:Molecular Weight; D009940:Organoids / Q000201:enzymology*; D051381:Rats; D013217:Starvation / Q000378:metabolism; D014503:Urate Oxidase / Q000032:analysis / Q000378:metabolism*
D000596:Amino Acids; D014503:Urate Oxidase