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Péptido — Preguntas frecuentes

Por Redacción · publicado 2026-04-08 · última revisión 2026-05-25 · Info

Si has estado leyendo sobre Péptido y quieres una sola página con lo útil —definiciones, contexto, cómo se estudia y las preguntas que se repiten—, es esta.

Esta página se actualizó el 2026-05-25 y se revisa periódicamente.

Evidencia disponible

(1996) Reverse micellar mass-transfer processes: spray column extraction of lysozyme. AIChE Journal, 42, 713-726. 100. Lienqueo, M.E., Leser, E.W. and Asenjo, J.A. (1996) An Expert System for the Selection and Synthesis of Multistep Protein Separation Processes. Comput. Chem. Engng., 20, S189-S194. 101. Schmidt, A.S., Andrews, B.A. and Asenjo, J.A. (1996) Correlations for the partition behaviour of proteins in aqueous two-phase systems. Effect of overall protein concentration. Biotechnol. Bioeng., 50, 617-626. 102. Asenjo, J.A., Sun, W-H. and Spencer, J.L. (1996) Optimal control of batch processes involving simultaneous enzymatic and microbial reactions. Bioproc. Engin., 14, 323-329. 103. Mistry, S.L., Kaul, A., Merchuk, J.C. and Asenjo, J.A. (1996) Mathematical Modelling and Computer Simulation of Aqueous Two-Phase Continuous Protein Extraction. J. Chromatography A, 741, 151-163. 104. Asenjo, J.A. and Chaudhuri, J.B. (1996) Innovative Separation Methods in Bioprocessing, in Separation Processes in the Food and Biotechnology Industries: Principles and Applications. Ed.: A.S. Grandison and M.J. Lewis, Woodhead Publ. Limited, Cambridge, U.K., p. 179-206. 105. Ferrer, P., Halkier, T., Hedegaard, L., Savva, D., Diers. I. and Asenjo, J.A. (1996) Nucleotide sequence of a β-1,3-glucanase isoenzyme IIA gene of Oerskovia xanthineolytica LL G109 (Cellulomonas cellulans) and initial characterization of the recombinant enzyme expressed in Bacillus subtilis. J. Bacteriology., 178, 4751-4757. 106. Parrado, J., Escuredo, P.R., Conejero-Lara, F. Kotik, M., Ponting, C.P., Asenjo, J.A.

Fuentes: es.wikipedia.org

Uso y manejo

and Dobson, C.M. (1996) Molecular characterisation of a thermoactive β-1,3-glucanase from Oerskovia xanthineolytica. Biochim. Biophys. Acta, 1296, 145-151. 107. Andrews, B.A. and Asenjo, J.A. (1996) Protein partitioning equilibrium between the aqueous PEG and salt phases and the solid protein phase in PEG/salt two-phase systems. J. Chromatography B, 685, 15-20. 108. Hachem, F., Andrews, B.A. and Asenjo, J.A. (1996) Hydrophobic partitioning of proteins in aqueous two-phase systems. Enzyme Microb. Technol., 19, 507-517. 109. Vazquez-Lima, F., Pyle, D.L. and Asenjo, J.A. (1997) Reaction kinetics of the esterification of lauric acid in iso-octane using an immobilized biocatalyst. Appl. Biochem. Biotechnol., 61, 411-422. 110. Andrews, B.A., Nielsen, S. and Asenjo, J.A. (1996) Partitioning and purification of monoclonal antibodies in aqueous two-phase systems. Bioseparation, 6, 303-313. 111. Harris, D.P., Andrews, A.T., Wright, G., Pyle, D.L. and Asenjo, J.A. (1997) The application of aqueous two-phase systems to the purification of pharmaceutical proteins from transgenic sheep milk. Bioseparation, 7, 31-37. 112. Rodrigues, M.I., Maciel-Filho, R., Asenjo, J.A., Zaror, C.A. and Maugeri, F. (1997) A procedure for feasible and optimal operational strategies for control of CARE systems. J. Chem.Technol. Biotechnol. , 69, 254-260. 113. Ferrer, P., Diers, I., Asenjo, J.A. and Andrews, B.A. (1998) Yeast cell permeabilizing β -1,3-glucanases: a tool for the integration of downstream processes and metabolic engineering applications to yeast. Biotechnol. Bioeng., 58, 321-324. 114.

Fuentes: es.wikipedia.org

Calidad y analítica

Merchuk, J.C., Andrews, B.A. and Asenjo, J.A. (1998) Aqueous two-phase systems for protein separation: studies on phase inversion. J. Chromatography, 711, 285-293. 115. Salamanca, M.H., Merchuk, J.C., Andrews, B.A. and Asenjo, J.A. (1998) On the kinetics of phase separation in aqueous two-phase systems. J. Chromatography, 711, 319-329. 116. Shene, C., Andrews, B.A. and Asenjo, J.A. (1999) Fed batch fermentations of Bacillus subtilis ToC46 (pPFF1) for the synthesis of a recombinant β-1,3- glucanase: Experimental study and modelling. Enz. Microb. Technol., 24, 247-254. 117. Huenupi,E., Gómez, A., Andrews, B.A. and Asenjo, J.A. (1999) Optimization and design considerations of two-phase continuous protein separation. J. Chem.Technol. Biotechnol., 74, 256-263. 118. Lienqueo, M.E., Salgado, J.C. and Asenjo, J.A. (1999) An Expert System for selection of protein purification processes: experimental validation. J. Chem. Technol. Biotechnol., 74, 293-299. 119. Salazar, O., Molitor, J.and Asenjo, J.A. (1999) Cloning and expression of an Oerskovia xanthineolytica –1,3-glucanase in Escherichia coli. Biotech. Letts., 21, 797-802. 120. Montagna, J.M., Vecchietti, A., Iribarren, O.A., Pinto J.M. and Asenjo, J.A. (2000) Optimal design of protein production plants with time and size factor process models. Biotechnol. Progress, 16, 228-237. 121. Shene, C., Mir, N., Andrews, B.A. and Asenjo (2000) Effect of the growth conditions on the synthesis of a recombinant -1,4-endoglucanase in continuous and fed-batch culture. Enz. Microb. Technol., 27, 248-253. 122. Graber, T.A., Andrews, B.A.

Fuentes: es.wikipedia.org

Páginas relacionadas en este sitio

Estabilidad y conservación

and Asenjo, J.A. (2000) Model for the partition of metal ions in aqueous two-phase systems. J. Chromatography B, 743, 57-64. 123. Taboada, M.E., Graber, T.A., Asenjo, J.A. and Andrews, B.A. (2000) Drowning-out crystallisation of sodium sulphate using aqueous two-phase systems. J. Chromatography B, 743, 101-105. 124. Asenjo, J.A., Montagna, J.M., Vecchietti, A.R., Iribarren, O.A. and Pinto, J.M. (2000) Strategies for the simultaneous optimization of the structure and the process variables of a protein production plant. Comput. Chem. Engng., 24, 2277-2290. 125. Lienqueo, M.E. and Asenjo, J.A. (2000) Use of expert systems for the synthesis of downstream protein processes. Comput. Chem. Engng., 24, 2339-2350. 126. Andrews, A.T., Harris, D.P., Wright, G, Pyle, D.L. and Asenjo, J.A. (2000) Affinity gel electrophoresis as a predictive technique in the fractionation of transgenic sheep milk proteins by affinity aqueous two-phase partitioning Biotechnol. Letts., 22, 1349–1353. 127. Taboada, M.E., Asenjo, J.A. and Andrews, B.A. (2001) Liquid-liquid and liquid-liquid-solid equilibria in PEG + Na2CO3 + water. Fluid Phase Equil., 108, 273-280. 128. Gonzalez, R., Asenjo, J.A. and Andrews, B.A. (2001) Metabolic control analysis of monoclonal antibody synthesis. Biotechnol. Progress., 17, 217-226. 129. Graber, T.A., Taboada, M.E., Andrews, B.A. and Asenjo, J.A. (2001) Influence of molecular weight of the polymer in the liquid-liquid equilibrium of the poly(ethylene glycol) + NaNO3 + H20 system at 298.15 K. J. Chem. Eng. Data., 46, 765 – 768. 130.

Fuentes: es.wikipedia.org

Preguntas frecuentes

¿Qué es Péptido?

Péptido se resume aquí a partir de literatura pública: definición, contexto y los puntos que se repiten en la práctica. Información general, no consejo médico.

¿Cómo se estudia Péptido en la literatura?

La investigación sobre Péptido se apoya sobre todo en estudios de laboratorio y en modelos animales; los datos clínicos varían según la sustancia. Reflejamos el estado de la literatura.

¿En qué fijarse con Péptido?

Lo decisivo son la pureza y la analítica (HPLC, espectrometría de masas), una reconstitución correcta y un almacenamiento adecuado.%!(EXTRA string=Péptido)

¿Qué incertidumbres hay con Péptido?

No todos los mecanismos están demostrados y un estudio aislado no es evidencia global. Esta página señala las preguntas abiertas en lugar de darlas por resueltas.%!(EXTRA string=Péptido)

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