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JBC, Vol. 250, Issue 17, 6756-6761, Sep, 1975
C. Ehnholm, W. Shaw, H. Greten and W. V. Brown
A triglyceride lipase different from lipoprotein lipase, but measurable
only after intravenous heparin injection, has been isolated from human
plasma by sequential use of heparin-Sepharose and concanavalin A-Sepharose
affinity chromatography. Using these procedures, phospholipase A1 activity
was found to chromatograph identically with the triglyceride lipase. The
constancy of the ratio of activities after isoelectric focusing (pI 4.1)
and during thermal deactivation indicates that this enzyme has hydrolase
activity against both triglycerides and phospholipids. This conclusion was
supported further by the homogeneity of the protein as indicated by sodium
dodecyl sulfate polyacrylamide gel electrophoresis.
Purification from human plasma of a heparin-released lipase with activity against triglyceride and phospholipids
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