Literature DB >> 7305952

An easy method for the determination of initial rates.

S G Waley.   

Abstract

When the Michaelis-Menten equation is obeyed, the rate near the beginning of an enzyme-catalyzed reaction (or of an experiment on transport) can be found accurately from the slope of a chord joining two points on the progress curve. This slope gives the rate at an intermediate concentration. Exact values of this intermediate concentration are easily calculated from equations in the text, and a number of values have also been tabulated. Methods of using two chords to find the initial rate are given. A mid-point formula for numerical differentiation is advocated when the Michaelis-Menten equation does not hold.

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Year:  1981        PMID: 7305952      PMCID: PMC1162697          DOI: 10.1042/bj1931009

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  13 in total

1.  The determination of the initial velocity of enzyme-catalysed reactions.

Authors:  R G Nicholls; A Jerfy; A B Roy
Journal:  Anal Biochem       Date:  1974-09       Impact factor: 3.365

2.  Use of progress curves to investigate product inhibition in enzyme-catalysed reactions. Application to the soluble mitochondrial adenosine triphosphatase.

Authors:  R D Philo; M J Selwyn
Journal:  Biochem J       Date:  1973-11       Impact factor: 3.857

3.  The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters.

Authors:  R Eisenthal; A Cornish-Bowden
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

4.  The reliability of Michaelis constants and maximum velocities estimated by using the integrated Michaelis-Menten equation.

Authors:  G L Atkins; I A Nimmo
Journal:  Biochem J       Date:  1973-12       Impact factor: 3.857

5.  Enzymic parameters: measurement of V and Km.

Authors:  H J Lee; I B Wilson
Journal:  Biochim Biophys Acta       Date:  1971-09-22

6.  The information content of enzyme kinetic data. 3. A comparison of four methods for fitting kinetic data to a power series.

Authors:  C Walter; M J Barrett
Journal:  Enzymologia       Date:  1970-03-31

7.  A simple method for calculating Km and V from a single enzyme reaction progress curve.

Authors:  S L Yun; C H Suelter
Journal:  Biochim Biophys Acta       Date:  1977-01-11

Review 8.  Current trends in the estimation of Michaelis-Menten parameters.

Authors:  G L Atkins; I A Nimmo
Journal:  Anal Biochem       Date:  1980-05-01       Impact factor: 3.365

9.  The determination of the initial velocities of enzyme-catalysed reactions from stopped-assay data [proceedings].

Authors:  G L Atkins; I A Nimmo
Journal:  Biochem Soc Trans       Date:  1978       Impact factor: 5.407

10.  An evaluation of methods for determining the initial velocities of enzyme-catalysed reactions from progress curves [proceedings].

Authors:  I A Nimmo; G L Atkins
Journal:  Biochem Soc Trans       Date:  1978       Impact factor: 5.407

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  16 in total

1.  Seasonal Changes in the Kinetic Parameters of a Photosynthetic Fructose-1,6-Bisphosphatase Isolated from Peltigera rufescens.

Authors:  D Brown; K A Kershaw
Journal:  Plant Physiol       Date:  1986-10       Impact factor: 8.340

2.  Detection of inhibition of 5-aminoimidazole-4-carboxamide ribotide transformylase by thioinosinic acid and azathioprine by a new colorimetric assay.

Authors:  T Ha; S L Morgan; W H Vaughn; I Eto; J E Baggott
Journal:  Biochem J       Date:  1990-12-01       Impact factor: 3.857

3.  Determination of initial velocities of enzymic reactions from progress curves.

Authors:  R Dagys; A Pauliukonis; D Kazlauskas; M Mankevicius; R Simutis
Journal:  Biochem J       Date:  1986-08-01       Impact factor: 3.857

4.  Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus.

Authors:  R Bicknell; S G Waley
Journal:  Biochem J       Date:  1985-10-01       Impact factor: 3.857

5.  The time course of hydrolysis of a beta-lactam antibiotic by intact gram-negative bacteria possessing a periplasmic beta-lactamase.

Authors:  W W Nichols
Journal:  Biochem J       Date:  1987-06-15       Impact factor: 3.857

6.  Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.

Authors:  C Garrido-del Solo; F García-Cánovas; B H Havsteen; R Varón-Castellanos
Journal:  Biochem J       Date:  1993-09-01       Impact factor: 3.857

7.  Cryoenzymology of trypsin. A detailed kinetic study of the trypsin-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester at low temperatures.

Authors:  J P Malthouse; A I Scott
Journal:  Biochem J       Date:  1983-12-01       Impact factor: 3.857

8.  The pH-dependence of class B and class C beta-lactamases.

Authors:  R Bicknell; V Knott-Hunziker; S G Waley
Journal:  Biochem J       Date:  1983-07-01       Impact factor: 3.857

9.  Inhibition of folate-dependent enzymes by non-steroidal anti-inflammatory drugs.

Authors:  J E Baggott; S L Morgan; T Ha; W H Vaughn; R J Hine
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

10.  Temperature-related kinetic differentiation of glucosephosphate isomerase alleloenzymes isolated from the blue mussel, Mytilus edulis.

Authors:  J G Hall
Journal:  Biochem Genet       Date:  1985-10       Impact factor: 1.890

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