01991naa a2200253 a 450000100080000000500110000800800410001910000180006024501640007826000090024252012240025165000190147565000100149465000140150465000230151865000150154165000170155665000120157365000150158565000150160070000170161570000160163277300890164815209452024-01-03 1977 bl uuuu u00u1 u #d1 aCHILLIARD, Y. aMise en évidence d'une activité lipoprotéine-lipasique dans le tissu adipeux de chèvrebcomparaison de trois méthodes d'extraction.h[electronic resource] c1977 aAbstract: Lipoprotein lipase activity in goat adipose tissue : comparison of three extraction methods. Lipoprotein lipase (L.P.L.) activity is studied in dairy goat omental adipose tissue and three methods of extracting it are compared. 1) in vitro incubation of tissue pieces in a medium containing heparin and goat serum (I.V. method). 2) homogenization in an ammoniacal buffer containing heparin (H.A. method). 3) homogenization of acetone-ether defatted powders in the ammoniacal buffer (E.A. method). These three types of crude extracts show lipolytic activity on « activated » lntralipid triglycerides. The effects of inhibitors and activators indicate that these activities are essentially due to enzyme L.P.L. Lipolytic activity is inhibited by an excess of substrate and has an apparent Km of 0.19 mM of the substrate triglyceride. Reproductibility of the successive steps of L.P.L. activity assay is estimated. Extraction by in vitro tissue incubation (LV, method) is less reproducible than the two other types of extraction (H.A. and E.A. methods). L.P.L. activity obtained by the 3 extraction methods is similar and highly correlated in the 13 tissue samples from 6 goats in different physiological states aAdipose tissue aGoats aLactation aLipoprotein lipase aPhysiology aReproduction aCaprino aFisiologia aLactação1 aDORLEANS, M.1 aFEHR, P. M. tAnnales de Biologie Animale, Biochimie, Biophysique,gv. 17, n. 1, p. 107-122, 1977.