作者: Torbjörn Egelrud , Thomas Olivecrona
DOI: 10.1016/S0021-9258(19)44784-4
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摘要: Abstract The purification of a lipase from skim milk is described. enzyme had the characteristics lipoprotein lipase, i.e. its activity against emulsified long chain triglyceride was stimulated more than 20-fold by addition suitable amounts serum to assay system and almost completely inhibited 1 m NaCl. After an initial fractionation milk, main obtained affinity chromatography on Sepharose 4B with covalently linked heparin. preparation purified 5,000- 7,000-fold. Gel electrophoresis this in urea or sodium dodecyl sulfate revealed one major component which stained for protein carbohydrate comprised 80% total protein. apparent minimum molecular weight 62,000 66,000 as determined polyacrylamide gels presence sulfate.