Separation of molecular species of lipoprotein lipase from adipose tissue.
نویسندگان
چکیده
When NH(4)OH-NH(4)Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. The first activity peak (LPL(a)) was eluted with an elution volume of a protein of molecular weight approximately five times that of the second (LPL(b)). Addition of heparin to the eluted fractions markedly stimulated activity of LPL(a), but suppressed that of LPL(b). 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.
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ورودعنوان ژورنال:
- Journal of lipid research
دوره 13 1 شماره
صفحات -
تاریخ انتشار 1972