Lipoprotein lipase in guinea pig tissues: molecular size and rates of synthesis.

Lipoprotein lipase was immunoprecipitated from guinea pig tissues which had been pulse labeled with [35S]methionine. The apparent size of the product (on SDS gels) was 55 kDa in all tissues studied. Lipoprotein lipase released by heparin from adipocytes and from perfused hearts had the same apparent size. No significant amounts of immunoreactive protein with smaller size were found on immunoblotting of tissue homogenates, or in preparations partially purified by heparin-Sepharose chromatography. Lipoprotein lipase accounted for only a small proportion of total protein synthesis. The highest value was in adipose tissue (0.3-0.8%). In lactating mammary gland lipoprotein lipase accounted for about 0.1%, a figure similar to that previously estimated for the proportion of lipoprotein lipase protein in milk. This suggests that lipoprotein lipase is secreted into milk as efficiently as other milk proteins are, in contrast to the previous opinion that the enzyme appears in milk because small amounts leak out from tissue sites. Relative synthesis of lipoprotein lipase was the same in adipocytes from fed or fasted animals, whereas relative synthesis of several other proteins changed dramatically. This indicates that some proteins in guinea pig adipose tissue are under transcriptional control in response to feeding-fasting, but that lipoprotein lipase is not.