Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Liliane Dupuis"'
Autor:
Robert Verger, Alain Roussel, Stéphane Canaan, Liliane Dupuis, Nabil Miled, Mireille Rivière, Frédéric Carrière, Christian Cambillau, De Caro A
Publikováno v:
Biochimie. 82:973-986
Human gastric lipase (HGL) is a lipolytic enzyme that is secreted by the chief cells located in the fundic part of the stomach. HGL plays an important role in lipid digestion, since it promotes the subsequent hydrolytic action of pancreatic lipase in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c685c1c356ed4f971dfd6a68fc09491
https://doi.org/10.1016/s0300-9084(00)01179-2
https://doi.org/10.1016/s0300-9084(00)01179-2
Autor:
Thierry Giardina, Véronique Raphel, Laetitia Guevel, Josette Perrier, Antoine Puigserver, Xiao-Jun Guo, Liliane Dupuis
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1432:371-381
Acylpeptide hydrolase was purified to homogeneity from porcine intestinal mucosa using a seven-step procedure including ammonium sulfate precipitation, gel filtration as well as anion exchange and affinity chromatography. The specific activity of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::392f1413e85e3fd7f5a074eef67273ce
https://doi.org/10.1016/s0167-4838(99)00087-4
https://doi.org/10.1016/s0167-4838(99)00087-4
Publikováno v:
European Journal of Biochemistry. 262:644-651
Human gastric lipase (HGL) is a highly glycosylated protein, as glycan chains account for about 15% of the molecular mass of the native HGL. Four potential N-glycosylation consensus sites (Asn15, 80, 252 and 308) can be identified from the HGL amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af5afa797832c49feb92a897035e8f7
https://doi.org/10.1046/j.1432-1327.1999.00427.x
https://doi.org/10.1046/j.1432-1327.1999.00427.x
Publikováno v:
Biochimie. 77:249-255
The first step in the set of reactions responsible for the biological utilization of L-2-hydroxy-4-methylthiobutanoic acid, the methionine hydroxy analogue, in protein synthesis was investigated in vitro using pure L-2-hydroxy acid oxidase A from chi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76b544c21fc959809c02eee4c1e275fe
https://doi.org/10.1016/0300-9084(96)88132-6
https://doi.org/10.1016/0300-9084(96)88132-6
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 105:503-507
1. L-2-HAOX A and L-2-HAOX B were purified from chicken and rat kidney with purification factors of 550 and 45, respectively. 2. It was established that both enzymes were tetrameric (M(r) = 169,000) and consisted of 40 kDa monomers. 3. While chicken
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83b2eac0ef9c243d7254d7df46f5f3aa
https://doi.org/10.1016/0305-0491(93)90080-o
https://doi.org/10.1016/0305-0491(93)90080-o
Publikováno v:
The Journal of Nutrition. 120:1171-1178
The peroxisomal enzyme L-2-hydroxy acid oxidase A (EC 1.1.3.1) was isolated from chicken liver to better evaluate its part in the utilization of the L isomer of supplemental DL-hydroxy-4-methylthiobutanoic acid by birds fed diets containing the methi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b17673190e66eeaa6bf6e080f3a871
https://doi.org/10.1093/jn/120.10.1171
https://doi.org/10.1093/jn/120.10.1171
Publikováno v:
Intestinal Lipid Metabolism ISBN: 9781461354352
Under normal physiological conditions the digestion and absorption of dietary lipids are highly efficiently processed. In humans, the diet generally contains 90 to 120 g of lipids (mostly triacylglycerols), more than 95% of which are absorbed, due to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca1c11af44a9fbd98ac946ca5d192776
https://doi.org/10.1007/978-1-4615-1195-3_2
https://doi.org/10.1007/978-1-4615-1195-3_2
Autor:
Robert Verger, Stéphane Canaan, Liliane Dupuis, Christian Cambillau, Mireille Rivière, Marie-Pierre Egloff, Alain Roussel
Publikováno v:
The Journal of biological chemistry. 274(24)
Fat digestion in humans requires not only the classical pancreatic lipase but also gastric lipase, which is stable and active despite the highly acidic stomach environment. We report here the structure of recombinant human gastric lipase at 3.0-A res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbc79f1dd93ce2f7458c2197deca95e4
https://pubmed.ncbi.nlm.nih.gov/10358049
https://pubmed.ncbi.nlm.nih.gov/10358049
Publikováno v:
Biochemical and biophysical research communications. 257(3)
Recombinant human gastric lipase (rHGL) and three of its cysteine mutants (cysteine 227, 236, and 244 substitued for threonine or serine) were expressed in the baculovirus/insect cell system and purified to homogeneity by performing a two-step proced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b905e65f8575cf518299b96eea15d9b5
https://pubmed.ncbi.nlm.nih.gov/10208872
https://pubmed.ncbi.nlm.nih.gov/10208872