Zobrazeno 1 - 10
of 166
pro vyhledávání: '"Ramón Varón"'
Autor:
María Llanos Amo-Saus, Manuela García-Moreno, Julio Escribano, Maria D. Masia, Ramón Varón, Carmen Vanessa Ortiz-Ruiz, Milagros Molina-Alarcón, Francisco García-Sevilla
Publikováno v:
Journal of Mathematical Chemistry. 54:1952-1972
In this paper we analyse the transient phase, i.e., the time course, of the fractional modification of monocyclic enzyme cascades with a more complete realistic definition for fractional modification as the fraction of the original enzyme converted i
Autor:
Ramón Varón, José Tudela, Carmen Vanessa Ortiz-Ruiz, Maria del Mar Garcia-Molina, Francisco García-Cánovas, Virginia Tomás, Miguel A. Maria-Solano
Publikováno v:
IUBMB Life. 67:757-767
The development of effective tyrosinase inhibitors has become increasingly important in the cosmetic, medicinal, and agricultural industries for application as antibrowning and depigmenting agents. The kinetic mechanisms of action of tyrosinase on mo
Autor:
Francisco García-Sevilla, Ramón Varón, Julio Escribano, Enrique Arribas, Milagros Molina-Alarcón, Maria D. Masia, María Llanos Amo-Saus, Manuela García-Moreno
Publikováno v:
Journal of Mathematical Chemistry. 52:2442-2458
This paper presents the discussion of a more complete definition of the fractional modification of an monocyclic enzyme cascade suggested, but not discussed, by Varon et al. (Bull Math Biol 68(7):1461-1493, 2006) as the quotient of the sum of all for
Autor:
Francisco García-Sevilla, M. Amo, Manuela García-Moreno, Maria D. Masia, Enrique Arribas, Ricardo Gomez-Ladron de Guevara, Ramón Varón, Milagros Molina-Alarcón, Maria del Mar Garcia-Molina
Publikováno v:
Journal of Mathematical Chemistry. 52:1647-1674
In this paper we extend to enzyme systems the results previously obtained in paper I of this series for linear compartmental systems. We obtain the time course equations for both the enzyme and ligand species involved in the reaction mechanisms, whic
Autor:
M. Amo, Manuela García-Moreno, Enrique Arribas, Ramón Varón, Ricardo Gomez-Ladron de Guevara, Maria del Mar Garcia-Molina, Maria D. Masia, Milagros Molina-Alarcón, Francisco García-Sevilla
Publikováno v:
Journal of Mathematical Chemistry. 52:1675-1689
Software application is implemented in this work to take full advantage of the characteristics of current operating systems and to provide the optimized symbolic kinetic equations for both enzyme and ligand species involved in enzyme reactions. This
Autor:
Mary of the Sea GARCÍA-MOLINA, Joseph Luis MUÑOZ-MUÑOZ, Joseph BERNA, Joseph Neptune RODRÍGUEZ-LÓPEZ, Ramón VARÓN, Francis GARCÍA-CÁNOVAS
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 77:2383-2388
Tyrosinase exists in three forms in the catalytic cycle depending on the oxidation state of the copper: met- (Em), oxy- (E(ox)), and deoxy- (Ed). When O-quinones, products of the enzymatic reaction, evolve chemically to generate an O-diphenol in the
Publikováno v:
In BioSystems 2000 56(2):75-82
Autor:
Milagros Molina-Alarcón, Manuela García-Moreno, María José García-Meseguer, Francisco García-Sevilla, Enrique Arribas, J. M. Villalba, Ramón Varón
Publikováno v:
Journal of Mathematical Chemistry. 50:1625-1648
Software has been implemented in this work to take full advantage of the characteristics of current operating systems and to provide the optimized symbolic kinetic equations for the linear compartmental systems derived in part I of this series. This
Autor:
Francisco García-Sevilla, J. M. Villalba, Enrique Arribas, Ramón Varón, Milagros Molina-Alarcón, Manuela García-Moreno, María José García-Meseguer
Publikováno v:
Journal of Mathematical Chemistry. 50:1598-1624
The study of many biological systems requires the application of a compartmental analysis, together with the use of isotopic tracers, parameter identification and methods to evaluate the mean parameters. For all this, the kinetic equations of the com
Autor:
Pedro Antonio García-Ruiz, Francisco Garcia-Molina, Jose Luis Muñoz-Muñoz, José Neptuno Rodríguez-López, Francisco García-Cánovas, Ramón Varón, José Tudela
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814:1974-1983
The kinetics of tyrosinase acting on o-aminophenols and aromatic amines as substrates was studied. The catalytic constants of aromatic monoamines and o-diamines were both low, these results are consistent with our previous mechanism in which the slow