Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Louis Sarda"'
Publikováno v:
International Journal of Peptide and Protein Research. 38:483-490
Comparison of the primary structures of pancreatic colipases from man, pig, horse and rat shows a high degree of homology between proteins. Fifty-two out of the 95 residues of the polypeptide are identical. All colipases contain 10 half-cystines whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b4cdf984d319dddacaf0568b12508af
https://doi.org/10.1111/j.1399-3011.1991.tb01530.x
https://doi.org/10.1111/j.1399-3011.1991.tb01530.x
Publikováno v:
European Journal of Biochemistry. 114:119-126
Porcine pancreatic colipase possesses a particular three-dimensional surface domain containing six out of the seven aromatic residues of the molecule in a highly hydrophobic environment [P. Canioni and P. Cozzone (1979) Biochimie (Paris) 61, 343–35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda2cabbe022e22ff6c7bd54e13456f3
https://doi.org/10.1111/j.1432-1033.1981.tb06181.x
https://doi.org/10.1111/j.1432-1033.1981.tb06181.x
Publikováno v:
Enzyme and Microbial Technology. 26:421-430
We have isolated a lipolytic strain from palm fruit that was identified as a Rhizopus oryzae. Culture conditions were optimized and highest lipase production amounting to 120 U/ml was achieved after 4 days of cultivation. The extracellular lipase was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fbe399d748e29fd13df583125f385a0
https://doi.org/10.1016/s0141-0229(99)00173-8
https://doi.org/10.1016/s0141-0229(99)00173-8
Autor:
Louis Sarda, Nathalie Rugani, Henri Chahinian, Louis-Claude Comeau, Aida Ibrik, Guillaume Vanot
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 64:215-222
Penicillium cyclopium, grown in stationary culture, produces a type I lipase specific for triacylglycerols while, in shaken culture, it produces a type II lipase only active on partial acylglycerols. Lipase II has been purified by ammonium sulfate pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2999c28604765cc5126ae350ce1097b
https://doi.org/10.1271/bbb.64.215
https://doi.org/10.1271/bbb.64.215
Publikováno v:
Lipids. 33:377-383
An extracellular lipase, active on water-insoluble triacylglycerols, has been isolated from Penicillium cyclopium. The purified enzyme has a molecular mass of 29 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis. It hydrolyzes emulsion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2882e6699435b61c51854c8e68ee4586
https://doi.org/10.1007/s11745-998-0218-6
https://doi.org/10.1007/s11745-998-0218-6
Autor:
Hugues Chap, François Leballe, Ashraf Ragab, Nathalie Rugani, Louis Sarda, Cécile Viodé, Marie-Françoise Simon, Bernard Fournié, Olivier Fourcade
Publikováno v:
Cell. 80:919-927
Nonpancreatic secretory phospholipase A 2 (sPLA 2 ) displays proinflammatory properties; however, its physiological substrate is not identified. Although inactive toward intact cells, sPLA 2 hydrolyzed phospholipids in membrane microvesicles shed fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a93c862d0bc2b5a1c794d5d0b459592f
https://doi.org/10.1016/0092-8674(95)90295-3
https://doi.org/10.1016/0092-8674(95)90295-3
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1247:185-194
Porcine colipase, the protein cofactor of pancreatic lipase, was isolated from pancreas freshly collected on animals and from a side fraction from the production of insulin (Novo Nordisk A/S). Samples of purified colipase were analyzed for homogeneit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92210a0f4cf6b6921a348ab660e1c7ef
https://doi.org/10.1016/0167-4838(94)00226-7
https://doi.org/10.1016/0167-4838(94)00226-7
Publikováno v:
European Journal of Biochemistry. 227:663-672
Procolipase is the precursor of colipase, which acts as protein cofactor for the activity of pancreatic lipase. The solution structure of procolipase has been determined by 1H NMR using two- and three-dimensional measurements. The secondary structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0063a410d95f213960110a17f9f9461a
https://doi.org/10.1111/j.1432-1033.1995.tb20186.x
https://doi.org/10.1111/j.1432-1033.1995.tb20186.x
Publikováno v:
Protein Science. 4:44-57
Colipase (Mr 10 kDa) confers catalytic activity to pancreatic lipase under physiological conditions (high bile salt concentrations). Previously determined 3-A-resolution X-ray structures of lipase-colipase complexes have shown that, in the absence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30cfb48bcd275a5efc4756dd1efa9325
https://doi.org/10.1002/pro.5560040107
https://doi.org/10.1002/pro.5560040107
Publikováno v:
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, Elsevier, 2010, 1801 (11), pp.1195-1204. ⟨10.1016/j.bbalip.2010.07.002⟩
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, 2010, 1801 (11), pp.1195-1204. ⟨10.1016/j.bbalip.2010.07.002⟩
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, Elsevier, 2010, 1801 (11), pp.1195-1204. ⟨10.1016/j.bbalip.2010.07.002⟩
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, 2010, 1801 (11), pp.1195-1204. ⟨10.1016/j.bbalip.2010.07.002⟩
International audience; To differentiate esterases from lipases at the structure-function level, we have compared the kinetic properties and structural features of sequence-related esterase 1 from rabbit liver (rLE) and bile-salt-activated lipase fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3466a0469a4749d8ecb1a7c54f78612
https://hal.inrae.fr/hal-02662436
https://hal.inrae.fr/hal-02662436
