A proteinous inhibitor of lipase was purified from soybean cotyledons by the procedures of ammonium sulfate fractionation, gel-filtration on Sephadex G-150 column, DEAE-cellulose column chromatography and isoelectric focusing. The inhibitor obtained by gelfiltration was separated into three active components, D-l, D-2 and D-3, by DEAE-cellulose column chromatography. The D-3 fraction after isoelectric focusing was homogeneous judged from disc electrophoresis. The inhibitory activity was more stable against treatments of heating and Pronase when the D-3 fraction was preincubated with substrate than without substrate. The extent of inhibition was varied by changing the order of addition of reactants and condition of substrate. From these results, the mode of inhibition is discussed.

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