Zobrazeno 1 - 10
of 265
pro vyhledávání: '"Robert Verger"'
Autor:
Yassine Ben Ali, Frédéric Carrière, Robert Verger, Stefan Petry, Günter Muller, Abdelkarim Abousalham
Publikováno v:
Journal of Lipid Research, Vol 46, Iss 5, Pp 994-1000 (2005)
Hormone-sensitive lipase (HSL) contributes importantly to the hydrolysis of cholesteryl ester in steroidogenic tissues, releasing the cholesterol required for adrenal steroidogenesis. HSL has broad substrate specificity, because it hydrolyzes triacyl
Externí odkaz:
https://doaj.org/article/aa7a21a9f8ef487d8bf4786155d22bfc
Publikováno v:
Journal of Lipid Research, Vol 40, Iss 12, Pp 2313-2321 (1999)
The aim of this study was to design a convenient, specific, sensitive, and continuous lipase activity assay using natural long-chain triacylglycerols (TAGs). Oil was extracted from Parinari glaberrimum seed kernels and the purified TAGs were used as
Externí odkaz:
https://doaj.org/article/2d11a7acdf5342b3b86a49fa081283bc
Autor:
Youssef Gargouri, Moncef M. Ladjimi, Habib Horchani, Robert Verger, Ali Chaari, Fakher Frikha
Publikováno v:
International Journal of Biological Macromolecules. 58:190-198
Due to the involvement of α-Synuclein (α-Syn) in lipid transport and its role in the normal function and in the pathology of Parkinson disease, it is important to study first the surface properties of the protein at the air/water interface and seco
Autor:
Yassine Ben Ali, Stefan Petry, Frédéric Carrière, Günter Müller, Robert Verger, Abdelkarim Abousalham
Publikováno v:
Biochimie. 94:137-145
Hormone-sensitive lipase (HSL) plays an important role in the mobilization of free fatty acids (FFA) from adipocytes. The inhibition of HSL may offer a pharmacological approach to reduce FFA levels in plasma and diminish peripheral insulin resistance
Publikováno v:
Journal of Colloid and Interface Science. 363:620-625
The interfacial kinetic and binding data for the pancreatic and intestinal sPLA2 from bird and mammals show that these enzymes have dramatically different ability to bind and hydrolyse phospholipids. The main conclusions from our experimental data in
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 86:71-80
The purpose of this article was to describe the kinetics of the enzymatic action of one or more enzymes on mixture of substrates organized in 2D structures in order to mimic some situations existing in biological or industrial systems. Hydrolysis of
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 62:19-26
The inhibitory effects of tetrahydrolipstatin (THL) on the hydrolytic activity of human pancreatic lipase (HPL) and T. lanuginosa lipase (TLL) on various lipidic substrates ‘poisoned’ with THL as previously described was studied, using either the
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 58:41-47
Tetrahydrolipstatin (THL, Orlistat) is a potent inhibitor of gastrointestinal lipases. Using the pH-stat technique we report that, in the absence of substrate, THL (at a molar excess of 100) inhibits rapidly (after few minutes of incubation) human pa
Publikováno v:
World Journal of Microbiology and Biotechnology. 25:1375-1384
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 67:107-114
The water-soluble lipolytic enzymes act at the interface of insoluble lipid substrates, where the catalytical step is coupled with various interfacial phenomena as enzyme penetration, solubilization of reaction products, loss of mechanical stability