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- W2079182595 abstract "A lipolytic acyl-hydrolase was purified 520-fold from an homogenate of potato leaves ( Solarium tuberosum L. cv. Benimaru). The purified enzyme showed a single protein band on polyacrylamide gel electrophoresis. The enzyme had an isoelectric point of 4.6 and a molecular weight of about 110 000. It had pH optima of 5.5 and 5.0, and K m values of 0.26 and 0.54 mM for monogalactosyldiacylglycerol and phosphatidylcholine, respectively. The pH dependences were altered by the addition of Triton X-100. No separation of these two hydrolyzing activities was achieved; the ratio of the specific activity of galactolipase to that of phospholipase (about 7 1 ) remained constant throughout the purification procedures. Both the activities were changed in parallel with each other by the addition of reagents and by heat treatment. The enzyme clearly catalyzed the deacylation of the several classes of galacto- and phospholipids. These results suggest that a single enzyme is responsible for both activities." @default.
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- W2079182595 date "1979-04-01" @default.
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- W2079182595 title "Purification and properties of a lipolytic acyl-hydrolase from potato leaves" @default.
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- W2079182595 doi "https://doi.org/10.1016/0005-2760(79)90182-6" @default.
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