コイ筋肉組織における細胞内酵素の分布および筋肉リソゾ-ムの性質について〔魚類筋肉組織のリソゾ-ム酵素に関する研究-2-〕

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The present work was undertaken to investigate the intracellular distribution of the enzymes such as cytochrome c oxidase (the mitochondrial marker), β-glucronidase, β-N-acetylglucosamini-dase, acid phosphatase and cathepsin D (the lysosomal markers), catalase (the peroxisomal marker) and alkaline phosphatase (the microsomal marker) in ordinary and dark muscles of carp according to differential centrifugation. Some particle properties of both muscle lysosomes were also examined. In the ordinary muscle, fractionation of total homogenate showed that all of the enzymes have the highest relative specific activity of cytochrome c oxidase, the four lysosomal enzymes and catalase and alkaline phosphatase were found in the mitochondrial, lysosomal and microsomal fractions, respectively. The buoyant densities of ordinary and dark muscle lysosomes were about 1.03%g/ml in iso-osmotic self-generating gradients composed of modified colloidal silica (PERCOLL), but a slight amount of lysosomes with higher buoyant density, about 1.04%g/ml, was found in dark muscle. The maximum stability of the muscle lysosomes was observed in sucrose over 0.2M and at pH 7. Temperature of incubation of dark muscle lysosomes in 0.25M sucrose had a slight effect on lysosomal-enzyme releases as compared to those from ordinary muscle. Carp muscle lysosomes were less stable than those from mammalian and chicken muscles when exposed to incubation at 37°C.
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