出版社：American Society for Biochemistry and Molecular Biology
摘要：Because we found apoprotein contamination of some high-grade commercial albumins, we studied this effect on formation of lipoprotein-like particles during lipolysis of human very low density lipoprotein (VLDL) in vitro. After a 1-hr incubation with purified bovine milk lipoprotein lipase, over 98% VLDL triglyceride was hydrolyzed in the presence of either albumin B (apoprotein-rich) or albumin C (apoprotein-poor), with a weight ratio of albumin to triglyceride of 60 to 1. Lipoproteins of density 1 with albumin C. All these differences can be ascribed to the presence in albumin B of 0.2 mg apoprotein A-I/g albumin and 1.8 mg phospholipid/g albumin; these components were not detected in albumin C. Thus, two thirds of "HDL" recovered with VLDL lipolysis in the presence of albumin B can be accounted for by albumin itself and only one third from constituents of VLDL. Adding equivalent amounts of both apoproteins removed from albumin B and phospholipid to albumin C markedly decreased the disparities in results but addition of each alone did not. These results prove "inert" albumins serve other than as fatty acid and lysolecithin acceptors in in vitro model systems, and do influence formation of lipoproteins during in vitro VLDL catabolism.-Deckelbaum, R. J., T. Olivecrona, and M. Fainaru. The role of different albumin preparations on production of human plasma lipoprotein-like particles in vitro.
