Purification and properties of two lipases from pig adipose tissue.
Two lipases were purified from pig adipose tissue after delipidation by a mild and effective procedure using mixtures of chloroform and butanol. This was followed by hydrophobic adsorption chromatography on aminohexyl-Sepharose 4B coupled with octanoic acid, gel filtration on Sephadex G-100, and isoelectric focusing. Two electrophoretically and chromatographically pure enzymes were obtained, which had the same molecular weight (60 000 +/- 3000) and specific activity, and almost identical amino acid compositions; the isoelectric points, i.e. 5.2 and 5.5, differed.
D000273:Adipose Tissue / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D013329:Structure-Activity Relationship; D013552:Swine
D000596:Amino Acids; D007527:Isoenzymes; D008049:Lipase