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Rat heart lipoprotein lipase.

J S Twu, A S Garfinkel, M C Schotz

    Atherosclerosis
    |November 1, 1975
    PubMed
    Summary

    Researchers purified rat heart lipoprotein lipase using heparin-Sepharose 4B affinity chromatography, achieving a 1500-fold purification. The enzyme

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Lipoprotein lipase (LPL) is a key enzyme in lipid metabolism.
    • Understanding LPL's properties is crucial for metabolic research.

    Purpose of the Study:

    • To highly purify rat heart lipoprotein lipase.
    • To characterize the biochemical properties of purified LPL.

    Main Methods:

    • Affinity chromatography using heparin-Sepharose 4B.
    • Disc gel electrophoresis for purity assessment.
    • Molecular weight determination.

    Main Results:

    • Lipoprotein lipase was purified 1500-fold with high recovery.
    • The enzyme exhibited a single protein band on disc gel electrophoresis.
    • Purified LPL required a serum cofactor (ApoLp-Glu substituted) for activity.
    • ApoLp-Ser, NaCl, and protamine sulfate inhibited activity, while heparin stimulated it.

    Conclusions:

    • Rat heart lipoprotein lipase can be highly purified using heparin-Sepharose 4B affinity chromatography.
    • The purified enzyme's activity is modulated by various factors, including cofactors and inhibitors.

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