Absence of mitochondrial terminal respiratory enzymes in cartilage matrix vesicles.
This study attempted to detect evidence of mitochondrial terminal respiratory components in matrix vesicles isolated from rachitic rat tibial epiphyseal plates. Biochemical assays for cytochrome c oxidase, NAD isocitrate dehydrogenase, NADP isocitrate dehydrogenase and succinate-cytochrome c reductase were negative. Polarimetric determinations revealed that the addition of succinate to matrix vesicles in suspension did not cause any increase in oxygen utilization. Spectrophotometric tracings of deoxycholate-solubilized matrix vesicles showed no characteristic absorption peaks or maxima belonging to any of the cytochrome complex components. Attempts to prepare pyridine hemochromes of cytochrome prosthetic groups from the matrix vesicles were also unsuccessful. The above results indicate that key components of mitochondrial respiratory systems are not detectable in rachitic matrix vesicles. The results are compatible with the interpretation that such vesicles are not derived from mitochondria.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002356:Cartilage / Q000032:analysis / Q000201:enzymology* / Q000648:ultrastructure; D003579:Cytochrome Reductases / Q000378:metabolism*; D003580:Cytochromes / Q000032:analysis; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007521:Isocitrate Dehydrogenase / Q000378:metabolism*; D009940:Organoids / Q000201:enzymology; D051381:Rats
D003580:Cytochromes; D007521:Isocitrate Dehydrogenase; D003579:Cytochrome Reductases; D003576:Electron Transport Complex IV; D000469:Alkaline Phosphatase