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- W1992704818 abstract "A technique is described for the purification of hog pancreatic lipase. This technique includes the following steps: aqueous extraction of hog pancreatin, fractional precipitations of the aqueous extract by ammonium sulfate and acetone, differential adsorptions on tricalcium phosphate and aluminum hydroxide, and finally zone electrophoresis at pH 5.25 in starch columns. A 135-fold purification is realized with a 20% over-all yield. The purest fraction appears to be electrophoretically and chromatographically homogeneous. There is probably a single lipase in hog pancreas. This lipase is able to act on tri-, di-, and monoglycerides, the reaction rate decreasing in this order. Its isoelectric point is about 5.2. The purest preparations give a typical protein spectrum. The turnover of the enzyme in the presence of bile salts at pH 9.0 and 37 °C. is at least 12 times its molecular weight. This means that, even if the molecular weight is as low as 25,000, the turnover of hog pancreatic lipase would be equal to or higher than 300,000. The high value of the turnover of an enzyme acting in a heterogeneous medium is readily explained by interactions of fundamental importance between lipase and insoluble esters." @default.
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- W1992704818 date "1959-07-01" @default.
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- W1992704818 title "Purification of hog pancreatic lipase" @default.
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- W1992704818 doi "https://doi.org/10.1016/0003-9861(59)90036-0" @default.
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