Simple numerical and graphical method to solve the kinetic parameters by dynamic thermogravimetry

1985 ◽  
Vol 91 ◽  
pp. 107-114 ◽  
Author(s):  
J. Ribas ◽  
M. Serra ◽  
A. Escuer
Keyword(s):  
Kinetic Parameters ◽  
Graphical Method ◽  
Dynamic Thermogravimetry

Graphical evaluation of the kinetic parameters for bacterial growth

1969 ◽  
Vol 15 (10) ◽  
pp. 1201-1205 ◽  
Author(s):  
Frank E. Stratton ◽  
Perry L. McCarty
Keyword(s):  
Kinetic Parameters ◽  
Bacterial Growth ◽  
Graphical Method ◽  
Substrate Oxidation ◽  
Kinetic Rate ◽  
Substrate Use ◽  
Oxidation Curve ◽  
Estimate Rate ◽  
Rates Of Growth

Kinetic rate parameters governing the rates of growth and substrate use by bacteria may be estimated by a graphical method which makes use of the bacterial substrate oxidation curve. The method is simple and rapid and may be used to estimate rate parameters in situations in which more precise computer estimates cannot be performed.

scholarly journals A method for determining kinetic parameters at high enzyme concentrations

1982 ◽  
Vol 203 (1) ◽  
pp. 339-342 ◽  
Author(s):  
C J Halfman ◽  
F Marcus
Keyword(s):  
Enzyme Activity ◽  
Kinetic Parameters ◽  
Graphical Method ◽  
Free Ligand ◽  
Enzyme Concentration ◽  
Fructose 1,6 Bisphosphatase ◽  
High Enzyme ◽  
Substrate Inhibitor ◽  
The Relationship

A graphical method is described which allows determination of kinetic parameters when substrate, inhibitor or activator concentrations must be in the vicinity of the enzyme concentration and a significant fraction of ligand is bound. Velocity is measured at several ligand: enzyme ratios at two or more enzyme concentrations. Results are obtained in terms of free and bound ligand corresponding to particular velocities. The relationship between velocity and bound and free ligand may then be analysed by any desired plotting technique. Preknowledge of the reaction mechanism or experimental determination of Vmax. is not required. The relationship between ligand bound and enzyme activity need not be linear and the method is equally suitable for analysing co-operative as well as simple kinetics. Application of the method is demonstrated by analysis of the inhibition of fructose, 1,6-bisphosphatase by AMP.

scholarly journals Effect of Mg2+ and Mn2+ on isocitrate lyase, a non-essentially metal-ion-activated enzyme. A graphical approach for the discrimination of the model for activation

1991 ◽  
Vol 276 (1) ◽  
pp. 223-230 ◽  
Author(s):  
E Giachetti ◽  
P Vanni
Keyword(s):  
Kinetic Parameters ◽  
Metal Ion ◽  
Graphical Method ◽  
Isocitrate Lyase ◽  
Enzyme Reaction ◽  
Activation Mechanism ◽  
Simple Method ◽  
Suggested Approach ◽  
Graphical Approach ◽  
Substrate Complex

We describe a simple method for the analysis of activation systems in which a metal ion modifier may combine with either the enzyme or the substrate (or both) and the metal ion-substrate complex is the true substrate of the enzyme reaction. The suggested approach is essentially a ‘graphical’ method that both provides unbiased criteria for the choice of the activation mechanism and yields good rough estimates of the kinetic parameters. The procedure, tested on a variety of simulated models, produces appropriate and reliable results. Applying this treatment to isocitrate lyase, we confirmed the data previously reported for Mg2+ [Giachetti, Pinzauti, Bonaccorsi & Vanni (1988) Eur. J. Biochem. 172, 85-92], and we found that Mn2+ functions with the same mechanism as does Mg2+, but with quite different kinetic constants. In particular, its ratio of the Vmax, values of the activated and the non-activated enzyme is less than 1, and thus Mn2+ is to be considered an inhibitor rather than an activator.

Relation of Statistically Significant, Abnormal, and Typical WAIS-R VIQ-PIQ Discrepancies to Full Scale IQs

2000 ◽  
Vol 16 (2) ◽  
pp. 107-114 ◽  
Author(s):  
Louis M. Hsu ◽  
Judy Hayman ◽  
Judith Koch ◽  
Debbie Mandell
Keyword(s):  
Graphical Method ◽  
The United States ◽  
Full Scale ◽  
True Score ◽  
Absolute Value ◽  
Normative Population ◽  
The Us ◽  
The Mean ◽  
And Performance ◽  
Quadratic Models

Summary: In the United States' normative population for the WAIS-R, differences (Ds) between persons' verbal and performance IQs (VIQs and PIQs) tend to increase with an increase in full scale IQs (FSIQs). This suggests that norm-referenced interpretations of Ds should take FSIQs into account. Two new graphs are presented to facilitate this type of interpretation. One of these graphs estimates the mean of absolute values of D (called typical D) at each FSIQ level of the US normative population. The other graph estimates the absolute value of D that is exceeded only 5% of the time (called abnormal D) at each FSIQ level of this population. A graph for the identification of conventional “statistically significant Ds” (also called “reliable Ds”) is also presented. A reliable D is defined in the context of classical true score theory as an absolute D that is unlikely (p < .05) to be exceeded by a person whose true VIQ and PIQ are equal. As conventionally defined reliable Ds do not depend on the FSIQ. The graphs of typical and abnormal Ds are based on quadratic models of the relation of sizes of Ds to FSIQs. These models are generalizations of models described in Hsu (1996) . The new graphical method of identifying Abnormal Ds is compared to the conventional Payne-Jones method of identifying these Ds. Implications of the three juxtaposed graphs for the interpretation of VIQ-PIQ differences are discussed.

MEASUREMENT OF STEROID BINDING PROTEINS

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom
Keyword(s):  
Kinetic Parameters ◽  
Binding Proteins ◽  
Binding Specificity ◽  
Binding Parameters ◽  
Target Organs ◽  
Biological Mixtures ◽  
Steroid Binding Proteins ◽  
Steroid Binding ◽  
Steroid Binding Protein

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.

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