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.