Characterization of a triglyceride hydrolase secreted by canine liver maintained in vitro.
These studies demonstrate that canine liver synthesizes a TGH activated by C-I but not by C-II. This TGH has properties similar to lipoprotein lipase C-I isolated from postheparin plasma of human subjects, but differs from a previously reported liver triglyceride-lipase or protamine insensitive-lipase in its sensitivity to NaCl and protamine sulfate, as well as in its requirement for a serum cofactor, C-I. These data suggest the possiblity that, in dogs, liver is a source of plasma LPLC-I.
D000818:Animals; D001059:Apoproteins / Q000494:pharmacology; D002914:Chylomicrons / Q000378:metabolism; D004285:Dogs; D004789:Enzyme Activation; D006493:Heparin / Q000008:administration & dosage; D066298:In Vitro Techniques; D008049:Lipase / Q000037:antagonists & inhibitors / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D008079:Lipoproteins, VLDL / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D011479:Protamines / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology
D001059:Apoproteins; D002914:Chylomicrons; D008079:Lipoproteins, VLDL; D011479:Protamines; D012965:Sodium Chloride; D006493:Heparin; D008049:Lipase