Abstract
A study has been made of the changes produced in the characteristics of the lipolytic activity of rat adipose tissue homogenates by prolonged preincubation of the intact tissue in phosphate buffer. Fresh tissue homogenates were markedly more active on a serum–triglyceride medium (activated substrate) than on triglyceride alone while little difference was noted with homogenates of preincubated tissue. The activity of fresh tissue homogenates was increased by addition of heparin; homogenates of incubated tissue were not affected. Fresh tissue homogenates were inhibited to a greater extent by protamine than were preparations of incubated material. Addition of glucose and insulin to the buffer partially maintained the activity of incubated tissue on activated substrate. These results indicate that while lipolytic activity of fresh rat adipose tissue has characteristics similar to lipoprotein lipase, the activity of incubated tissue differs from this enzyme in several respects. This study demonstrates the lability of lipoprotein lipase in rat adipose tissue and suggests the presence in this tissue of a separate type of lipolytic activity.
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