scholarly journals Sigmoid curves, non-linear double-reciprocal plots and allosterism

1975 ◽  
Vol 149 (2) ◽  
pp. 313-328 ◽  
Author(s):  
W G Bardsley ◽  
R E Childs
Keyword(s):  
Steady State ◽  
Kinetic Data ◽  
Initial Rate ◽  
Plane Curves ◽  
British Library ◽  
Mathematical Significance ◽  
Steady State Kinetic ◽  
Non Linear ◽  
State Kinetic ◽  
Maximum Utilization

1. The theory of plane curves was applied to the graphical methods used in enzyme kinetics and a mathematical analysis of the possible graph shapes is given. 2. The belief that allosterism can be inferred from steady-state data alone is subjected to criticism and the mathematical significance of sigmoid curves and non-linear double-reciprocal plots is explored. 3. It is suggested that the usual methods of interpreting steady-state kinetic data are often based on over-restrictive assumptions which prevent maximum utilization of the available data. 4. Methods for obtaining the degree of the rate equation from graph shapes obtained directly from initial-rate measurements and from replots of asymptotic behaviour as x → 0 and x → ∞ are discussed. 5. Detailed proofs of the theorems given in the text have been deposited as Supplementary Publication SUP 50049 (10 pages) at the British Library (Lending Division), Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.

Calibration of glucose biosensors by using pre-steady state kinetic data

1998 ◽  
Vol 13 (7-8) ◽  
pp. 801-807 ◽  
Author(s):  
Toonika Rinken ◽  
Ago Rinken ◽  
Toomas Tenno ◽  
Jaak Järv
Keyword(s):  
Steady State ◽  
Kinetic Data ◽  
Glucose Biosensors ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Co-operativity and the methods of plotting binding and steady-state kinetic data

1978 ◽  
Vol 171 (2) ◽  
pp. 501-504 ◽  
Author(s):  
E P Whitehead
Keyword(s):  
Steady State ◽  
Ligand Binding ◽  
Substrate Concentration ◽  
Kinetic Data ◽  
Free Ligand ◽  
Free Energies ◽  
Steady State Kinetic ◽  
Second Derivatives ◽  
The Hill ◽  
State Kinetic

The features that distinguish positive from negative co-operativity in double-reciprocal Eadie-Hofstee-Scatchard and Hanes plots, often incorrectly stated to be the sign of curvature or second derivatives, are explained. It is shown how to determine the ‘Hill exponent’ and interaciton free energies from curves in these plots, and in the simple plot of ligand binding or velocity against free ligand or substrate concentration. New types of plots, where the kind of co-operative behaviour is more obvious than in the traditional ones, are proposed.

scholarly journals Pre-steady-state kinetic analysis of damage recognition by human single-strand selective monofunctional uracil-DNA glycosylase SMUG1

2017 ◽  
Vol 13 (12) ◽  
pp. 2638-2649 ◽  
Author(s):  
Alexandra A. Kuznetsova ◽  
Danila A. Iakovlev ◽  
Inna V. Misovets ◽  
Alexander A. Ishchenko ◽  
Murat K. Saparbaev ◽  
...  
Keyword(s):  
Steady State ◽  
Kinetic Analysis ◽  
Kinetic Data ◽  
Single Strand ◽  
Dna Glycosylase ◽  
Uracil Dna Glycosylase ◽  
Damage Recognition ◽  
Steady State Kinetic ◽  
State Kinetic

The mechanism of damaged base recognition by hSMUG1 was elucidated using comparison of pre-steady state kinetic data obtained by Trp and aPu fluorescence and FRET detection.

scholarly journals Computer program for the kinetic equations of enzyme reactions. The case in which more than one enzyme species is present at the onset of the reaction

1991 ◽  
Vol 278 (1) ◽  
pp. 91-97 ◽  
Author(s):  
R Varón ◽  
B H Havsteen ◽  
M García ◽  
F García-Canóvas ◽  
J Tudela
Keyword(s):  
Steady State ◽  
Computer Program ◽  
Enzyme System ◽  
Kinetic Equations ◽  
British Library ◽  
Transient Phase ◽  
Enzyme Reactions ◽  
Steady State Kinetic ◽  
State Kinetic ◽  
Enzyme Species

This paper presents an extension of the program developed by Varón, Havsteen, García, García-Cánovas & Tudela [(1990) Biochem. J. 270, 825-828] for the expression of the transient-phase and steady-state kinetic equations of a general enzyme system in which the only enzyme species present at the onset of the reaction is the free enzyme. The program has been extended to situations in which more than one enzyme species may be present at the onset of the reaction. The program is given in Supplementary Publication SUP50165 (5 pages), which has been deposited at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1991) 273, 5.

scholarly journals Isolation and properties of cytochrome c peroxidase from Pseudomonas denitrificans

1979 ◽  
Vol 181 (1) ◽  
pp. 159-169 ◽  
Author(s):  
A F W Coulson ◽  
R I C Oliver
Keyword(s):  
Molecular Weight ◽  
Absorption Spectrum ◽  
Steady State ◽  
Cytochrome C ◽  
Kinetic Data ◽  
Cytochrome C Peroxidase ◽  
Pseudomonas Denitrificans ◽  
Steady State Kinetic ◽  
Cytochromes C ◽  
State Kinetic

The isolation of cytochrome c peroxidase, cytochrome c4, cytochrome c-551 and azurin from Pseudomonas dentrificans is described. The peroxidase has a molecular weight of 63,000 and an isoelectric point of 5.6. Its absorption spectrum suggests that it contains two haem c groups/molecule. Preliminary steady-state kinetic data are reported with cytochromes c-551 and c4 and azurin as the second substrate.

scholarly journals Steady-state kinetic studies of the inhibitory action of Zn2+ on ribonuclease T1 catalysis

1982 ◽  
Vol 207 (2) ◽  
pp. 357-362 ◽  
Author(s):  
M Itaya ◽  
Y Inoue
Keyword(s):  
Steady State ◽  
Kinetic Data ◽  
Kinetic Studies ◽  
Kinetic Mechanism ◽  
Ribonuclease T1 ◽  
Steady State Kinetic ◽  
Competitive Action ◽  
Dinucleoside Monophosphates ◽  
State Kinetic ◽  
Apparent Equilibrium

The kinetic mechanism of specific inhibition by Zn2+ of ribonuclease T1 catalysis was studied by steady-state kinetic analysis of transphosphorylation of dinucleotides, GpCp(3′), GpUp(2′) and GpUp(3′), and dinucleoside monophosphates, GpC and GpU. The inhibition was not simply competitive, non-competitive or uncompetitive, but the kinetic data were compatible with a mechanism of ‘fully mixed inhibition’ in which a fully non-competitive action was associated with a partially competitive action. Apparent equilibrium quotients involved in this model of inhibition were determined for the dinucleotide substrates, and we found that binding of either of Zn2+ and substrate was facilitated when the other was bound. The location of Zn2+ was suggested to be near His-40 and/or His-92 of the ribonuclease T1 molecule.

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