Autores comunican |
(especial para SIIC © Derechos reservados) |
| Cristian Ruiz * Autor invitado por SIIC |
|
Descripción de la investigación |
Barcelona, España (especial para SIIC): |
Cristian Ruiz * |
|
| Referencias bibliográficas | |
| 1 S. Higaki, Lipase inhibitors for the treatment of acne, J. Mol. Catal., B
Enzym. 22 (2003) 377– 384.
2 A. Slomiany, B.L. Slomiany, Synthesis and macromolecular organization of gastrointestinal mucin, J. Physiol. Pharmacol. 43 (1992) 115–138. 3 L.M. Lichtenberger, The hydrophobic barrier properties of gastrointestinal mucus, Annu. Rev. Physiol. 57 (1995) 565– 583. 4 D.T. Smoot, How does Helicobacter pylori cause mucosal damage? direct mechanisms, Gastroenterology 113 (1997) S31-34,50. 5 B.L. Slomiany, J. Piotrowski, A. Slomiany, Effect of sucralfate on the degradation of human gastric mucus by Helicobacter pylori protease and lipases, Am. J. Gastroenterol. 87 (1992) 595– 599. 6 B.L. Slomiany, V.L. Murty, J. Piotrowski, A. Slomiany, Gastroprotective agents in mucosal defense against Helicobacter pylori, Gen. Pharmacol. 25 (1994) 833–841. 7 S. Benjamin, A. Pandey, Candida rugosa lipases: molecular biology and versatility in biotechnology, Yeast 14 (1998) 1069–1087. 8 J.W. Simons, R.C. Cox, M.R. Egmond, H.M. Verheij, Rational design of alpha-keto triglyceride analogues as inhibitors for Staphylococcus hyicus lipase, Biochemistry 38 (1999) 6346–6351. 9 F. Beisson, A. Tiss, C. Riviere, R. Verger, Methods for lipase detection and assay: a critical review, Eur. J. Lipid Sci. Technol. 28 (2000) 133– 153. 10 D. Wahler, J.L. Reymond, Novel methods for biocatalyst screening, Curr. Opin. Chem. Biol. 5 (2001) 152– 158. 11 N. Prim, A. Blanco, J. Martinez, F.I.J. Pastor, P. Diaz, EstA, a gene coding for a cell-bound esterase from Paenibacillus sp. BP-23, is a new member of the bacterial subclass of type B carboxylesterases, Res. Microbiol. 151 (2000) 303–312. 12 A.L. Colombo, A.S. Melo, R.F. Crespo Rosas, R. Salomao, M. Briones, R.J. Hollis, S.A. Messer, M.A. Pfaller, Outbreak of Candida rugosa candidemia: an emerging pathogen that may be refractory to amphotericin B therapy, Diagn. Microbiol. Infect. Dis. 46 (2003) 253– 257. 13 K.-E. Jaeger, B.W. Dijkstra, M.T. Reetz, Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases, Annu. Rev. Microbiol. 53 (1999) 315– 351. 14 V. Khalameyzer, I. Fischer, U.T. Bornscheuer, J. Altenbuchner, Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones, Appl. Environ. Microbiol. 65 (1999) 477–482. 15 C. Ruiz, F.I.J. Pastor, P. Diaz, Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species, Lett. Appl. Microbiol. 37 (2003) 354– 359. 16 T. Eggert, G. van Pouderoyen, B.W. Dijkstra, K.-E. Jaeger, Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional struc-ture, FEBS Lett. 502 (2001) 89– 92. 17 T. Eggert, U. Brockmeier, M.J. Droge, W.J. Quax, K.-E. Jaeger, Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH, FEMS Microbiol. Lett. 225 (2003) 319– 324. 18 M. Markweg-Hanke, S. Lang, F. Wagner, Dodecanoic acid inhibition of a lipase from Acinetobacter sp. OPA 55, Enzyme Microb. Technol. 17 (1995) 512–516. 19 S. Hari Krishna, N.G. Karanth, Lipase-catalyzed synthesis of iso-amyl butyrate, a kinetic study, Biochim. Biophys. Acta 1547 (2001) 262– 267. 20 C.Q. Sun, C.J. O’Connor, A.M. Robertson, Antibacterial actions of fatty acids and monoglycerides against Helicobacter pylori, FEMS Immunol. Med. Microbiol. 36 (2003) 9– 17. 21 A. Ruzin, R.P. Novick, Equivalence of lauric acid and glycerol monolaurate as inhibitors of signal transduction in Staphylococcus aureus, J. Bacteriol. 182 (2000) 2668– 2671. 22 N. Prim, F.I.J. Pastor, P. Diaz, Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7, Curr. Microbiol. 42 (2001) 237– 240. 23 J. Zock, C. Cantwell, J. Swartling, R. Hodges, T. Pohl, K. Sutton, P. Rosteck Jr, D. McGilvray, S. Queener, The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli, Gene 151 (1994) 37– 43. 24 V. Dartois, A. Baulard, K. Schanck, C. Colson, Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168, Biochim. Biophys. Acta 1131 (1992) 253– 260. 25 C. Ruiz, A. Blanco, F.I.J. Pastor, P. Diaz, Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase, FEMS Microbiol. Lett. 217 (2002) 263– 267. 26 T. Eggert, G. Pencreac’h, I. Douchet, R. Verger, K.-E. Jaeger, A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase, Eur. J. Biochem. 267 (2000) 6459– 6469. 27 G. Iacazio, C. Perissol, B. Faure, A new tannase substrate for spectrophotometric assay, J. Microbiol. Methods 42 (2000) 209– 214. 28 E. Grippa, R. Valla, L. Battinelli, G. Mazzanti, L. Saso, B. Silvestrini, Inhibition of Candida rugosa lipase by berberine and structurally related alkaloids, evaluated by high-performance liquid chromatography, Biosci. Biotechnol. Biochem. 63 (1999) 1557– 1562. 29 O. Redondo, A. Herrero, J.F. Bello, M.G. Roig, M.V. Calvo, F.J. Plou, F.J. Burguillo, Comparative kinetic study of lipases A and B from Candida rugosa in the hydrolysis of lipid p-nitrophenyl esters in mixed micelles with Triton X-100, Biochim. Biophys. Acta. 1243 (1995) 15– 24. 30 M. Sanchez, N. Prim, F. Randez-Gil, F.I.J. Pastor, P. Diaz, Engineering of baker’s yeasts, E. coli and Bacillus hosts for the production of Bacillus subtilis Lipase A, Biotechnol. Bioeng. 78 (2002) 339–345. 31 K. Edwards, R.Y. Chan, W.H. Sawyer, Interactions between fatty acids and lipoprotein lipase: specific binding and complex formation, Biochemistry 33 (1994) 13304–13311. 32 M. Cygler, J.D. Schrag, Structure and conformational flexibility of Candida rugosa lipase, Biochim. Biophys. Acta 1441 (1999) 205–214. 33 A. Larsson, C. Erlanson-Albertsson, Effect of phosphatidylcholine and free fatty acids on the activity of pancreatic lipase-colipase, Biochim. Biophys. Acta 876 (3) (1986) 543–550. 34 M.C. Bano, H. Gonzalez-Navarro, C. Abad, Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water – lipid interface, Biochim. Biophys. Acta 1632 (1 –3) (2003) 55– 61. 35 L. Alberghina, R. Gnandori, S. Longhi, M. Loti, Molecular cloning of a lipase and of a lipase related gene from Candida cylindricea, in: L. Alberghina, R.D. Schmid, R. Verger (Eds.), Lipases: Structure, Mechanism and Genetic Engineering, GBF-Monographs vol. 16, 1991, pp. 231–235. |
|
| Otros
artículos de Cristian Ruiz N. Prim, A. Blanco, J. Martinez, F.I.J. Pastor, P. Diaz, EstA, a gene coding for a cell-bound esterase from Paenibacillus sp. BP-23, is a new member of the bacterial subclass of type B carboxylesterases, Res. Microbiol. 151 (2000) 303– 312. C. Ruiz, F.I.J. Pastor, P. Diaz, Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species, Lett. Appl. Microbiol. 37 (2003) 354– 359. N. Prim, F.I.J. Pastor, P. Diaz, Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7, Curr. Microbiol. 42 (2001) 237– 240. C. Ruiz, A. Blanco, F.I.J. Pastor, P. Diaz, Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase, FEMS Microbiol. Lett. 217 (2002) 263– 267. E. Grippa, R. Valla, L. Battinelli, G. Mazzanti, L. Saso, B. Silvestrini, Inhibition of Candida rugosa lipase by berberine and structurally related alkaloids, evaluated by high-performance liquid chromatography, Biosci. Biotechnol. Biochem. 63 (1999) 1557– 1562. M. Sanchez, N. Prim, F. Randez-Gil, F.I.J. Pastor, P. Diaz, Engineering of baker’s yeasts, E. coli and Bacillus hosts for the production of Bacillus subtilis Lipase A, Biotechnol. Bioeng. 78 (2002) 339–345. Prim, N., Sánchez, M., Ruiz, C., Pastor, F.I.J., Diaz, P. (2003). Use of methylumbeliferyl-derivative substrates for lipase activity characterization. J. Mol. Cat. B-Enz. 22:339-346. Firuzi O, Giansanti L, Vento R, Seibert C, Petrucci R, Marrosu G, Agostino R, Saso L. (2003) Hypochlorite scavenging activity of hydroxycinnamic acids evaluated by a rapid microplate method based on the measurement of chloramines. J Pharm Pharmacol. 55(7):1021-7. Bonanni G, Saso L.(2003) Evaluation of the adherence to the asthma guidelines by the administration of a questionnaire in community pharmacies. Minerva Med. 2003 Feb;94(1):29-40. Ruiz C, Falcocchio S, Xoxi E, Javier Pastor FI, Diaz P, Saso L (2004). Activation and inhibition of Candida rugosa and Bacillus-related lipases by saturated fatty acids, evaluated by a new colorimetric microassay. Biochim Biophys Acta1672(3):184-191. |
|
Para comunicarce con Cristian Ruiz mencionar a SIIC como referencia: Av. Diagonal 645, 08028, Barcelona, Catalunya, España Fono: 93 4034627; Fax: 93 4034629 pdiaz@ub.edu |
|
|
Acerca del trabajo completo |
|
Título en castellano ACTIVACION E INHIBICION POR ACIDOS GRASOS SATURADOS DE LAS LIPASAS DE CANDIDA RUGOSA Y DE ESPECIES RELACIONADAS CON BACILLUS, EVALUADAS MEDIANTE UN NUEVO MICROENSAYO COLORIMETRICO |
Autores |
|
1 Estudiante de Doctorado, Departamento
de Microbiología. Universidad de Barcelona, Investigador Contratado 2 Investigadora, Department of Pharmacology of Natural Substances and General Physiology, Univers, Investigadora Contratada 3 Estudiante de Doctorado, Department of Pharmacology of Natural Substances and General Physiology, Becaria Investigación 4 Biólogo, Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona, Profesor Titular de Universidad 5 Bióloga, Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona, Profesora Titular de Universidad 6 Farmaceutico, Department df Pharmacology df Natural Substances and General Physiology, Univers, Académico/ Investigador |
Acceso a
la fuente original |
Acceso al texto original
completo |
Acceso al resumen/ abstract
original |
Acceso a la cita en
Medline |
Clasificado en siicsalud |
|
|
|
Acerca de SIIC Estructura de SIIC Sociedad
Iberoamericana de Información Científica (SIIC) |