Separation of molecular species of lipoprotein lipase from adipose tissue

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). A...

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Bibliographic Details
Published in:Journal of Lipid Research
Main Authors: Arlene S. Garfinkel, Michael C. Schotz
Format: Article
Language:English
Published: Elsevier 1972-01-01
Subjects:
gel filtration
heparin
serum activation
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520394372
Description
Summary: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.
ISSN:0022-2275

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