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- W2084654017 abstract "A homogeneous preparation of the enzyme that catalyses triacylglycerol synthesis has been achieved for the first time from plant tissue. Diacylglycerol acyltransferase (EC 2.3.1.20) was solubilized from purified microsomes prepared from germinating soybean (Glycine max L. Merr. cv. Dare) cotyledons with the non denaturing zwitterionic detergent, CHAPS. The enzyme was isolated from CHAPS solubilized microsomal proteins and purified by Sepharose CL-4B chromatography and agarose gel electrophoresis. Purified diacylglycerol acyltransferase exhibited a single Schlieren image during analytical ultracentrifugation. The homogeneity of the enzyme was confirmed by high-pressure liquid chromatography using gel filtration columns. The purified enzyme was devoid of lipase (EC 3.1.1.3), glycerolphosphate acyltransferase (EC 2.3.1.15), lysolecithin acyltransferase (EC 2.3.1.23), acylglycerol acyltransferase (EC 2.3.1.22), and 1-acylglycerolphosphate acyltransferase (EC 2.3.1.51) activities. Purified diacylglycerol acyltransferase activity was stable for three months at −20°C. Hyperbolic enzyme kinetics were observed using sn-1,2-diolein and stearoyl-CoA or oleoyl-CoA as substrates. The apparent Km using sn-1,2-diolein was 60 μM with stearoyl-CoA, and 113 μM with oleoyl-CoA. This report has documented a method by which highly purified diacylglycerol acyltransferase may be obtained from germinating soybean cotyledons." @default.
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- W2084654017 date "1986-06-01" @default.
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- W2084654017 title "Isolation and purification of diacylglycerol acyltransferase from germinating soybean cotyledons" @default.
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- W2084654017 doi "https://doi.org/10.1016/0005-2760(86)90300-0" @default.
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