PMID: 6476376Jun 1, 1984

A method for determining binding kinetics applied to thiamine-binding protein

Analytical Biochemistry
H NishimuraA Iwashima


A rapid and simple method for assaying the binding activity of thiamine-binding protein is described. By this assay method, the binding characteristics of rice bran thiamine-binding protein have been evaluated with [14C]thiamine as ligand. Analysis of these data by Scatchard plot resulted in linear plots giving a dissociation constant (Kd) for thiamine of 0.55 microM and a maximum binding (Bmax) of 14.5 pmol of ligand bound/microgram of protein. Thiamine binding to the binding protein was time dependent and reached equilibrium at approximately 20 min. The Kob was 0.18 min-1 and the k1 was 1.25 X 10(5) min-1 M-1. Reversibility of thiamine binding at equilibrium was completed at 60 min with a k2 value of 0.052 min-1. The Kd calculated from the reverse rate constant was 0.42 microM. These results indicated that this binding assay method was substantially reliable and accurate.


Mar 27, 1979·Biochimica Et Biophysica Acta·A Iwashima, H Nishimura
Nov 2, 1979·Biochimica Et Biophysica Acta·A IwashimaY Nose
May 1, 1973·Analytical Biochemistry·T Nishimune, R Hayashi
Feb 1, 1984·Journal of Nutritional Science and Vitaminology·H NishimuraA Iwashima

Related Concepts

Thiamine-binding protein
Carrier Proteins
Plant Proteins
Plasma Protein Binding Capacity
Rice (Dietary)
Thiamine Mononitrate

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