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- W2024744341 abstract "It appears that the recently established capacity of rat liver homogenates to hydrolyze long-chain triglycerides [ 1,2] is due primarily to the presence of a lysosomal lipase with an acidic pH optimum [3-51 and a microsomal lipase exhibiting maximal activity at alkaline pH values [6,7] . There is less conclusive evidence for the presence of another distinct lipase in the plasma membrane [4,89] as well as an inactive lipoprotein lipase [lo] . However, it has also been proposed [ 1 l] that liver lipase is a complex of liver esterase and lipid rather than a separate enzyme. Some of these conflicting results indicate clearly the necessity for further studies on the characterization and differentiation of liver lipolytic enzymes which obviously play a very significant role not only in intracellular catabolism but also in the uptake of triglycerides by the liver. This communication describes the pH optima, time courses of hydrolysis and the effects of various compounds on the pig liver lipolytic activities and presents the evidence for their subcellular localization." @default.
- W2024744341 created "2016-06-24" @default.
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- W2024744341 date "1970-09-24" @default.
- W2024744341 modified "2023-09-26" @default.
- W2024744341 title "Long-chain triglyceride lipases of pig liver" @default.
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- W2024744341 doi "https://doi.org/10.1016/0014-5793(70)80430-6" @default.
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