title: [Isolation and properties of triglyceride lipase from the rabbit liver].
abstract: Using affinity chromatography on heparin-Sepharose 4B, triglyceride lipase was isolated from rabbit liver tissue and purified. The specific activity of the enzyme isolated from the usual homogenate was equal to (3.8 +/- 1.2) x 10(3) mumol/hour/mg protein. After treatment of liver tissue homogenates with liquid nitrogen the enzyme activity increased severalfold as compared to the enzyme isolated from the usual homogenate. The dependences of the triglyceride lipase activity on the concentrations of the protein (enzyme), substrate (triglyceride), albumin (fatty acid acceptor) and pH were studied. The isolated form of liver triglyceride lipase was found to have two pH optima at 6.5 and 8.5.
authors.forename: N G
authors.initials: NG
authors.lastname: Nikul'cheva
authors.forename: I B
authors.initials: IB
authors.lastname: Soliternova
authors.forename: L A
authors.initials: LA
authors.lastname: Eliseeva
mesh_terms: D000418:Albumins; D000818:Animals; D002846:Chromatography, Affinity; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D009584:Nitrogen; D011817:Rabbits; D013379:Substrate Specificity
chemical_list: D000418:Albumins; D003470:Culture Media; D008049:Lipase; D009584:Nitrogen
vernacular_title: Vydelenie i svoĭstva triglitseridlipazy pecheni krolika.