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J Kinderlerer

Publications and source records attributed to J Kinderlerer.

23 records · Page 2Linked to original sources
PubMed1976

The derivation of second degree rate equations arising from two-substrate, two-product enzyme catalysed reactions whose catalytic cycle is branched.

A selection of two-substrate, two-product enzyme catalysed reactions with alternate catalytic cycles and second degree rate equations was examined by the computer program described by Kinderlerer and Ainsworth (1976). It is shown that the numerator terms of the rate equations are particularly simple, easy to derive and capable of creating a broad division of the mechanisms considered. THE NUMERATOR TERMS ALSO HAVE THE ADVANTAGE OF BEING UNAFFECTED BY DEAD END INHIBITION OR THE PRESENCE OF Theorell-Chance reactions. It is then shown that the relatively small group of mechanisms, isolated by the numerator analysis, can be distinguished from each other by considering the denominator terms of the rate equation that are second degree in the concentration of the varied substrate.

Catalysis↗
PubMed1975

A computer program for deriving the rate equations of enzyme catalysed reactions with unbranched mechanisms.

This paper describes a simple program for a desk-top computer which determines the relative concentrations of enzyme-containing intermediates appearing in an enzyme catalysed reaction where the intermediates lie in an unbranched sequence originating and terminating in one enzyme intermediate. This information, the distribution function, then gives the rate equation by the usual means (Wong and Hanes, 1962). The method is rapid and has the advantage that the distribution function may be presented in its complete form or in terms of its dependence on the concentration of the substrates and products. It is also possible to determine the effects of dead-end inhibition.

Computers↗
PubMed1973

The thermal denaturation of human oxyhaemoglobins A, A2, C and S.

1. The time-courses of thermal denaturation of human oxyhaemoglobins A, A(2), C and S at 45 degrees C were studied by following the increase in protein fluorescence. Haemoglobins S and C were less stable than haemoglobin A, whereas haemoglobin A(2) was considerably more stable. 2. The time-courses of denaturation did not follow first-order kinetics and could be fitted most simply to a co-operative scheme in which the partial denaturation of the alpha chain preceded that of the beta chain. 3. The denaturation of these haemoglobins was studied as a function of temperature by using optical rotatory dispersion. Haemoglobin A(2) was again more stable than the others. The addition of small quantities of haemoglobin A(2) had a disproportionate effect on the stability of haemoglobin C. 4. The thermodynamic parameters of the denaturation process were calculated.

Hemoglobin C↗
PubMedDate not supplied

Location of critical points in the reaction velocity/concentration relationships predicted by the exponential model for a two substrate regulatory enzyme.

The two substrate exponential model for a regulatory enzyme (Ainsworth and Gregory, J. Theor. Biol., 75 (1978) 97-114) can be employed to describe non-hyperbolic relationships between the initial velocity of the catalysed reaction and the concentration of one substrate when the concentration of the second substrate is kept constant, v = f(A)B. The model equation for v = f(A)B predicts the possibility of a maximum, catastrophe and inflections but, because the equation is transcendental, it is not possible to locate the critical points by algebraic analysis. The paper describes an iterative computer program that has been devised to solve this problem.

Catalysis↗