Characterization of serum-stimulated lipoprotein lipase from bovine heart.
1. A triglyceride (TG) lipase is present in whole homogenate and tissue extracts of beef myocardium with characteristics of lipoprotein lipase (LPL); i.e., activity is stimulated by serum, inhibited by NaCl and protamine sulfate, the protein binds to heparin-Sepharose, and the enzyme has an alkaline pH optimum. 2. This TG lipase, eluted from heparin-Sepharose at 0.9-1.0 M NaCl, has an apparent mol. wt of 64 K daltons. Its primary mRNA is 3.7 kb. 3. Expression of LPL mRNA and enzyme activities are in the ratio of approximately 20:8:1 for hearts of mouse, rat and beef, respectively and correlate with r = +0.99.
LaDu
M J
MJ
Department of Physical Education, University of Illinois, Chicago 60680.
Schultz
C J
CJ
Essig
D A
DA
Palmer
W K
WK
D000818:Animals; D002417:Cattle; D066298:In Vitro Techniques; D008071:Lipoprotein Lipase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D013045:Species Specificity
D012333:RNA, Messenger; D008071:Lipoprotein Lipase