Publications by the researcher in collaboration with Jose Bautista Tudela Serrano (16)

1992

  1. Analysis of a kinetic model for melanin biosynthesis pathway

    Journal of Biological Chemistry, Vol. 267, Núm. 6, pp. 3801-3810

1989

  1. 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

  1. Kinetic study in the transient phase of the suicide inactivation of frog epidermis tyrosinase

    Biophysical Chemistry, Vol. 30, Núm. 3, pp. 303-310

  2. 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

  1. 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

  2. Kinetic characterization of dopamine as a suicide substrate of tyrosinase

    Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 2, Núm. 1, pp. 47-56

  3. 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

  4. 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

  5. Kinetics of a general model for enzyme activation through a limited proteolysis

    Mathematical Biosciences, Vol. 87, Núm. 1, pp. 31-45

  6. L-mimosine a slow-binding inhibitor of mushroom tyrosinase

    Phytochemistry, Vol. 26, Núm. 4, pp. 917-919

  7. 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

  8. 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

  1. 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

  2. Determination of the kinetic constants of inhibited acetyl cholinesterase

    Italian Journal of Biochemistry, Vol. 35, Núm. 4, pp. 259-265

  3. 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

  4. Study of α-methyldopa oxidation by tyrosinase

    International Journal of Biochemistry, Vol. 18, Núm. 1, pp. 39-47