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- W1967874143 abstract "A proteinaceous inhibitor of lipase was isolated and partially purified from confectionery and high-oil type sunflower seed (Helianthus annuus L.) by ammonium sulphate fractionation. The 50 % of saturation fraction contained most of the proteinaceous lipase inhibitor activity from both seed types. Gel chromatography of dialysed preparations of this fraction indicated that the inhibitor protein has a Mr of ca 70 000 determined from calculated distribution coefficients (Kd) on G-150 and G-200 Sephadex columns. Complete inhibition of hog pancreas and C. cylindracea lipases was achieved when mixed 1: 1 (v/v) with the sunflower protein, even though substrate specificity for these two lipases was significantly different on cottonseed and olive oils. The sunflower protein was a competitive inhibitor of C. cylindracea lipase during lipolysis of sunflower oil. The apparent Vm determined from the inhibited and uninhibited reactions was 5.5 x 10−6 mol FFA/sec/mg protein. The apparent Km determined for the uninhibited reaction with sunflower oil was 4.1 M and 6.2 M for the inhibited reaction. The formation of a tightly-bound inhibitor protein-lipase complex probably occurred since free fatty acid composition was unaltered during lipolysis in the inhibited reaction and oil substrate inhibition was approximately the same in both inhibited and uninhibited reactions." @default.
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- W1967874143 date "1987-01-01" @default.
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- W1967874143 title "A proteinaceous competitive inhibitor of lipase isolated from Helianthus annuus seeds" @default.
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- W1967874143 doi "https://doi.org/10.1016/s0031-9422(00)82455-3" @default.
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