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Journal of Lipid Research, Vol. 13, 63-68, January 1972
Copyright © 1972 by Lipid Research, Inc.

Separation of molecular species of lipoprotein lipase from adipose tissue

Arlene S. Garfinkel and Michael C. Schotz

Research, Veterans Administration Hospital (Wadsworth), Los Angeles, California 90073, and Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024

When NH4OH-NH4Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. The first activity peak (LPLa) was eluted with an elution volume of a protein of molecular weight approximately five times that of the second (LPLb). Addition of heparin to the eluted fractions markedly stimulated activity of LPLa, but suppressed that of LPLb. Both lipases had the characteristics that distinguish lipoprotein lipase from other tissue lipases: a requirement for serum for substrate activation, inhibition by 1 m NaCl, and an alkaline pH optimum (pH 8.0). It is concluded that these fractions represent two species of lipoprotein lipase.

Supplementary key words gel filtration • heparin • serum activation

Submitted on May 24, 1971
Accepted on August 5, 1971


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