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Journal of Lipid Research, Vol. 21, 425-434, May 1980
Copyright © 1980 by Lipid Research, Inc.

The role of different albumin preparations on production of human plasma lipoprotein-like particles in vitro

Richard J. Deckelbaum , Thomas Olivecrona , and Menahem Fainaru

Gastroenterology Unit and Lipid Research Laboratory, Department of Medicine B, Hadassah University Hospital, Hebrew University-Hadassah Medical School, Jerusalem, Israel, and Department of Medical Chemistry, University of Umea, Umea, Sweden

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 < 1.019 g/ml ("IDL"), 1.019 to 1.063 g/ml ("LDL"), and 1.063 to 1.21 g/ml ("HDL") were then isolated by ultracentrifugation. Recovery of non-triglyceride VLDL constituents in "IDL" and "LDL" was similar for albumin B or albumin C. "LDL" was the major catabolic product of in vitro VLDL lipolysis independent of the albumin used. The yield of "HDL," however, was 5- to 6-fold greater with albumin B. All lipoproteins produced with albumin B were richer in phospholipid, apoproteins C and A-I, relative to lipoproteins produced in the presence of albumin C. With albumin B, cholesterol/phospholipid molar ratios were <1 in all in vitro produced lipoproteins, but were >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.

Supplementary key words albumin contaminants • very low density lipoprotein catabolism

Submitted on July 5, 1979
Revised on November 2, 1979

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