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- W2017702999 abstract "1. The pre-heparin plasma of the rat, and the perfusate obtained from isolated rat liver following perfusion with heparin, showed lipolytic activities principally against monoglyceride and tributyrin substrates, and minor triglyceride and diglyceride hydrolase activities. Rates of activity with 1- and 2-monoglycerides were similar. 2. Each activity in these preparations was characterised by resistance to inhibition by NaCl and protamine, and by sensitivity to inhibition by diethyl p-nitrophenyl phosphate. The pH optimum was 7.25–7.4 for the different lipid substrates. 3. Purified lipoprotein lipase, the post-heparin perfusate of extrahepatic tissues and whole post-heparin plasma were characterised by major lipolytic activities against di- and triglycerides, and by monoglyceride hydrolase activity directed mainly against the I-isomer. Each activity was strongly inhibited by NaCI and by protamine, and was comparatively resistant to inhibition by diethyl p-nitrophenyl phosphate. pH optima were 8.0–8.3 for the different lipid substrates, in the presence of whole serum as activator. 4. A principal function of the monoglyceride hydrolase activity of pre-heparin plasma, and released from the liver by heparin, may be to hydrolyse the 2-monoglyceride residue, which is the major product of lipoprotein lipase activity against triglyceride substrates." @default.
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- W2017702999 title "Further characterisation of lipoprotein lipase and hepatic post-heparin lipase from rat plasma" @default.
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- W2017702999 doi "https://doi.org/10.1016/0005-2760(72)90137-3" @default.
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