Affinity chromatography on heparin-sepharose of rat adipose tissue triglyceride lipase from cytosol.
Subfractionation of the fat free homogenate of rat adipose tissue showed that a high yield of triglyceride lipase was recovered reproducibly in the microsomal supernatant fraction (cytosol) when rat epididymal fat pads were homogenized in sucrose-EDTA-Tris medium. Triglyceride lipase was bound on heparin-Sepharose. Hydrolyzing activity towards triacylglycerol was eluted as a single, sharp peak in 0.7 M NaCl, 5 mM sodium barbital and 20% glycerol (pH 7.0). The triglyceride lipase was not inhibited by 1 M NaCl and not stimulated by the presence of fresh human serum. A lipoprotein-lipase activity was demonstrable in the cytosol when adipose tissue from fed rats were used. Fasting of the animals lowered this activity.
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology; D006493:Heparin; D008049:Lipase / Q000302:isolation & purification*; D008297:Male; D051381:Rats; D012685:Sepharose; D013347:Subcellular Fractions / Q000201:enzymology; D014280:Triglycerides
D014280:Triglycerides; D006493:Heparin; D012685:Sepharose; D008049:Lipase