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A novel transient phase kinetic analysis of the fractional modification of monocyclic enzyme cascades.
- Published in:
- Journal of Mathematical Chemistry, 2016, v. 54, n. 10, p. 1952, doi. 10.1007/s10910-016-0659-y
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- Article
Analysis of the fractional modification of the monocyclic enzyme cascades, defined in an alternative way involving the two forms of the modified protein.
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- Journal of Mathematical Chemistry, 2014, v. 52, n. 9, p. 2442, doi. 10.1007/s10910-014-0392-3
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- Article
Linear compartmental systems. III. Application to enzymatic reactions.
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- Journal of Mathematical Chemistry, 2014, v. 52, n. 7, p. 1647, doi. 10.1007/s10910-014-0360-y
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- Article
Linear compartmental systems. IV. A software, under MS-Windows, for obtaining the instantaneous species concentrations in enzyme systems.
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- Journal of Mathematical Chemistry, 2014, v. 52, n. 7, p. 1675, doi. 10.1007/s10910-014-0361-x
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- Article
Linear compartmental systems: II-A software to obtain the symbolic kinetic equations.
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- Journal of Mathematical Chemistry, 2012, v. 50, n. 6, p. 1625, doi. 10.1007/s10910-012-9992-y
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- Article
Linear compartmental systems. I. kinetic analysis and derivation of their optimized symbolic equations.
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- Journal of Mathematical Chemistry, 2012, v. 50, n. 6, p. 1598, doi. 10.1007/s10910-012-9991-z
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- Article
Kinetics of intra- and intermolecular zymogen activation with formation of an enzyme–zymogen complex.
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- FEBS Journal, 2005, v. 272, n. 1, p. 85, doi. 10.1111/j.1432-1033.2004.04400.x
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- Article
Kinetics of autocatalytic zymogen activation measured by a coupled reaction: pepsinogen autoactivation.
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- Biological Chemistry, 2005, v. 386, n. 7, p. 689, doi. 10.1515/BC.2005.080
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- Article
Kinetic Analysis of an Autocatalytic Process Coupled to a Reversible Inhibition: The Inhibition of the System Trypsinogen-Trypsin by p-Aminobenzamidine.
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- Biological Chemistry, 1995, v. 376, n. 9, p. 577
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- Article
Kinetic Analysis of the Opened Bicyclic Enzyme Cascades.
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- Biological Chemistry, 1994, v. 375, n. 6, p. 355
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- Article
Final Phase of Enzyme Reactions Following a Michaelis-Menten Mechanism in which the Free Enzyme and/or the Enzyme-Substrate Complex are Unstable.
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- Biological Chemistry, 1994, v. 375, n. 1, p. 35
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- Article