Jose Bautista
Tudela Serrano
Catedraticos de Universidad
Publicaciones en las que colabora con Francisco Garcia Carmona (16)
1992
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Analysis of a kinetic model for melanin biosynthesis pathway
Journal of Biological Chemistry, Vol. 267, Núm. 6, pp. 3801-3810
1989
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A kinetic study of the suicide inactivation of an enzyme measured through coupling reactions. Application to the suicide inactivation of tyrosinase
Biochemical Journal, Vol. 262, Núm. 2, pp. 597-603
1988
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Kinetic study in the transient phase of the suicide inactivation of frog epidermis tyrosinase
Biophysical Chemistry, Vol. 30, Núm. 3, pp. 303-310
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Kinetics of a model for zymogen activation: The case of high activating enzyme concentrations
Journal of Theoretical Biology, Vol. 132, Núm. 1, pp. 51-59
1987
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Kinetic characterization of an enzymatic irreversible inhibition measured in the presence of coupling enzymes. The inhibition of adenosine triphosphatase from sarcoplasmic reticulum by fluorescein isothiocyanate
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 911, Núm. 2, pp. 256-260
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Kinetic characterization of dopamine as a suicide substrate of tyrosinase
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 2, Núm. 1, pp. 47-56
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Kinetic study of the transient phase of a chemical reaction system coupled to an enzymatically catalyzed step. Application to the oxidation of epinine by tyrosinase
Biophysical Chemistry, Vol. 27, Núm. 1, pp. 15-25
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Kinetic study on the suicide inactivation of tyrosinase induced by catechol
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 912, Núm. 3, pp. 417-423
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Kinetics of a general model for enzyme activation through a limited proteolysis
Mathematical Biosciences, Vol. 87, Núm. 1, pp. 31-45
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L-mimosine a slow-binding inhibitor of mushroom tyrosinase
Phytochemistry, Vol. 26, Núm. 4, pp. 917-919
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Mechanistic origin of the kinetic cooperativity for the ATPase activity of sarcoplasmic reticulum
Journal of Bioenergetics and Biomembranes, Vol. 19, Núm. 4, pp. 383-396
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Transient-phase kinetics of enzyme inactivation induced by suicide substrates
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 912, Núm. 3, pp. 408-416
1986
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A kinetic study of the irreversible inhibition of an enzyme measured in the presence of coupled enzymes. Fluorescein isothiocyanate as inhibitor of the adenosinetriphosphatase activity from sarcoplasmic reticulum
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 869, Núm. 1, pp. 8-15
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Determination of the kinetic constants of inhibited acetyl cholinesterase
Italian Journal of Biochemistry, Vol. 35, Núm. 4, pp. 259-265
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Irreversible inhibition of trypsin by tlck. A continuous method for kinetic study of irreversible enzymatic inhibitors in the presence of substrate
International Journal of Biochemistry, Vol. 18, Núm. 3, pp. 285-288
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Study of α-methyldopa oxidation by tyrosinase
International Journal of Biochemistry, Vol. 18, Núm. 1, pp. 39-47