Characterization of the lipoprotein lipase in the functional pool of rat heart by immunoblotting.
Rat hearts were perfused with heparin for 2 min at 4 degrees C. The lipoprotein lipase activity in the perfusate was inhibited by antiserum to rat adipose tissue lipoprotein lipase. By immunoblotting, the lipoprotein lipase derived from the functional pool of the heart was found to be a protein with an apparent Mr of 69 000. After incubation of the perfusate at 37 degrees C for 24 h an immunologically reactive protein with an apparent Mr of 28 000 was found. This protein is not a physiological derivative of the enzyme but a degradation product.
D000818:Animals; D007163:Immunosorbent Techniques; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D010477:Perfusion; D051381:Rats
D008071:Lipoprotein Lipase