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Enzymatic Activity in Mitochondria from Orobanche
Author(s) -
SINGH PRIKHSHAYAT,
KRISHNAN P. S.
Publication year - 1977
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1977.tb01511.x
Subject(s) - malate dehydrogenase , biochemistry , isocitrate dehydrogenase , succinate dehydrogenase , mitochondrion , biology , aconitase , cytochrome c oxidase , fumarase , dehydrogenase , enzyme , glyoxylate cycle , branched chain alpha keto acid dehydrogenase complex , glutamate dehydrogenase , glutamate receptor , receptor
Mitochondria from Orobanche were analysed for the activities of aconitate hydratase, isocitrate dehydrogenase, succinate dehydro‐genase, fumarate hydratase, malate dehydrogenase, NADH oxidase, substrate‐cytochrome c oxidoreductases, glutamate dehydrogenase, aminotransferases, ATPase and “malic” enzyme. The specific activities of isocitrate dehydrogenase, NADH oxidase, substrate‐cytochrome c oxidoreductases and glutamate dehydrogenase in the mitochondria) fraction from parasite tissue compared favourably with those reported for most of the mitochondria from growing and storage tissues. Succinate dehydrogenase, fumarate hydratase and aspartate aminotransferase were of intermediate activity, while aconitate hydratase and malate dehydrogenase had rather low activity, and “malic” enzyme had very low activity in comparison with other preparations. The relevance of these findings in relation to mitochondrial metabolism in the parasite is discussed. No evidence was obtained to suggest any basic abnormality in the biochemical properties of the mitochondria from Orobanche centua which may be correlated with its obligatorily parasitic existence.