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- W1987299710 abstract "1. A high yield of triglyceride lipase was recovered reproducibly in the clear 105000 × g supernatant (S105 fraction) when rat epididymal fat pads were homogenized in 0.25 M sucrose containing 10−3 M EDTA. 2. Previous exposure of intact fat pads to epinephrine (5 · 10−5 M) caused an increment in the triglyceride lipase activity recovered in the S105 fraction. 3. This hormone-sensitive lipase activity was not inhibited by 1 M NaCl or protamine sulfate (800 μg/ml). NaF (10−2 M) inhibited the activity by 80%. 4. A part of the lipase activity floated during preparative ultracentrifugation at medium densities greater than 1.125. Previous treatment of the intact fat pads with epinephrine increased the activity in this floating (d < 1.125) fraction. 5. Lipase activity in the S105 fraction was rapidly inactivated during incubation at 37° and pH 7.4. This deactivation could be blocked by 10−3 M EDTA. 6. After 35-fold purification of lipase, obtained by precipitation at pH 5.2 and preparative ultracentrifugation at d = 1.125, the enzyme was stable even in the absence of EDTA. 7. A high level of lipoprotein lipase activity was demonstrable in the S105 fraction when fat pads from fed rats were used. Fasting of the animals or preincubation of fat pads in glucose-free medium lowered this activity without changing the activity of the hormone-sensitive triglyceride lipase." @default.
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- W1987299710 date "1970-11-01" @default.
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- W1987299710 title "Partial purification and characterization of hormonesensitive lipase from rat adipose tissue" @default.
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- W1987299710 doi "https://doi.org/10.1016/0005-2760(70)90152-9" @default.
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