1965
DOI: 10.1016/0005-2787(65)90559-9
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Phospholipid-protein interaction as a determinant for the substrate specificity of mitochondrial nicotinamide-adenine-dinucleotide (phosphate) transhydrogenase

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1966
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Cited by 17 publications
(2 citation statements)
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“…Lipase is reversibly adsorbed on the substrate surface, and bile salts enhance the rate of this reversible reaction (300). A change in the specificity of NADPH:NAD oxldoreductase of rat heart mitochondria has been noted upon treatment of the enzyme with phospholipase A or with lipid solvents (302). A number of polar lipids replace the naturally occurring ricinoleic acid tetramer.…”
Section: Lipid Functionsmentioning
confidence: 99%
See 1 more Smart Citation
“…Lipase is reversibly adsorbed on the substrate surface, and bile salts enhance the rate of this reversible reaction (300). A change in the specificity of NADPH:NAD oxldoreductase of rat heart mitochondria has been noted upon treatment of the enzyme with phospholipase A or with lipid solvents (302). A number of polar lipids replace the naturally occurring ricinoleic acid tetramer.…”
Section: Lipid Functionsmentioning
confidence: 99%
“…Another lipase, the acid lipase of 2~icinus comrnunis, hydrolyzes long chain saturated glycerides in the presence of a cyclic tetramer of ricinoleic acid, but not after the enzyme has been extracted with butanol (301). In this instance the conformation of the enzyme may be changed by treatment (302). Since polar lipids are not required for the hydrolysis of water-soluble tributyrin, the lipid factor probably allows formation of a suitable enzyme-substrate complex.…”
Section: Lipid Functionsmentioning
confidence: 99%