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Studies in vitro of lipogenesis in rat testicular tissue
Author(s) -
Whorton A. R.,
Coniglio J. G.
Publication year - 1975
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532321
Subject(s) - biochemistry , dehydrogenase , pyruvate carboxylase , enzyme , malic enzyme , fatty acid synthesis , lipogenesis , atp citrate lyase , malate dehydrogenase , fatty acid , citrate synthase , branched chain alpha keto acid dehydrogenase complex , acetyl coa , biology , chemistry , metabolism
Testicular tissue was shown to contain the full complement of enzymes required for de novo synthesis of fatty acids. The enzymes capable of snythesizing palmitic acid from citrate, acetate, or acetyl CoA were found to be present in the soluble (cytoplasmic) fraction. These included fatty acid synthetase, acetyl CoA carboxylase, citrate‐cleavage enzyme, malic enzyme, glucose‐6‐phosphate dehydrogenase, and 6‐phosphogluconate dehydrogenase. Optimal conditions for assaying activities of fatty acid synthetase and acetyl CoA carboxylase in the soluble fraction from rat testes were established, and the activities of these two enzymes were determined to be 0.54±0.1 and 0.030±0.002 (nmoles of substrate incorporated into fatty acid per min per mg of soluble fraction protein), respectively. The activities of citrate‐cleavage enzyme, malic enzyme, and the glucose‐6‐phosphate dehydrogenase/6‐phosphogluconate dehydrogenase pair were also measured. The activities were 6.0±0.7, 34.9±4.2, and 29.9±9.3 nmoles/min/mg, respectively.