Summary
The activities of peroxisomal enzymes of rat liver were followed 1 to 10 days after subtotal (60–70%) hepatectomy in homogenates prepared from regenerating livers and in cell fractions isolated from them.
Catalase activity was found to be depressed in the total liver homogenate (H) as well as in the mitochondrial (M) and soluble (S) fractions, while it did not change appreciably in the microsomal (Mc) and lysosomal (L) fractions, α-hydroxyacid oxidase behaved in a similar fashion. In contrast to these enzymes, urate oxidase activity remained unchanged in H, whereas it was decreased in M and increased in L and Mc during the first 5 days after operation. These results agree well with the assumption that microbody proliferation is initiated by the fragmentation of large peroxisomes. The different relations of peroxisomal enzyme activities during regeneration time are discussed with respect to the possible existence of various kinds of peroxisomes with different enzyme equipments and with different turnover rates.
Biochemical examinations were paralleled to morphological and histochemical studies. An early increase in number of peroxisomes was found to occur during the first day after partial hepatectomy, which is accompanied by decrease in particle size. During the first mitotic wave (24–36 hrs post op.) the number of peroxisomes per cell was reduced to about the half. After this time number and size of the particles began to increase.
Positive staining of ribosomes was frequently observed in the vicinity of peroxisomes after the application of the cytochemical catalase reaction (alkaline diaminobenzidine medium). This phenomenon is interpreted to represent rather a diffusion artifact that the cytochemical identification of newly synthesized catalase.
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Goldenberg, H., Hüttinger, M., Böck, P. et al. Influence of subtotal hepatectomy on peroxisomes and peroxisomal enzymes of rat liver and isolated liver cell fractions. Histochemistry 44, 47–56 (1975). https://doi.org/10.1007/BF00490420
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DOI: https://doi.org/10.1007/BF00490420