PMID: 6737095Feb 1, 1984

Purification and some properties of thiamine-binding protein from rice bran

Journal of Nutritional Science and Vitaminology
H NishimuraA Iwashima

Abstract

A thiamine-binding protein was purified from the extract of rice bran acetone powder by conventional procedures of acid precipitation, a series of column chromatography on DEAE-Sephadex A-50 and DEAE-cellulose, and gel filtration of Sephadex G-200. The purified thiamine-binding protein was nearly homogeneous as judged by disc gel electrophoresis and the molecular weight was estimated to be 94,000 by gel filtration on Sephadex Gn-200 and 50,000 by sodium dodecylsulfate (SDS) gel electrophoresis, suggesting that the protein is composed of two identical subunits. The apparent Kd and Bmax of the binding for [14C]thiamine was 0.44 +/- 0.05 microM and 17.2 +/- 0.7 nmol/mg of protein, respectively. The optimal pH for the binding is between 8.0 and 9.0. From the competition experiment using several thiamine derivatives, high binding specificity of the protein for thiamine was presumed.

Citations

Mar 31, 2004·Plant Physiology and Biochemistry : PPB·Anna GołdaM Rapała-Kozik
Oct 18, 2016·Current Opinion in Biotechnology·Aymeric Goyer
Jun 1, 1984·Analytical Biochemistry·H NishimuraA Iwashima
Mar 25, 2020·Critical Reviews in Biotechnology·Hasthi RamTilak Raj Sharma

Related Concepts

Thiamine-binding protein
Carrier Proteins
Chromatography, DEAE-Cellulose
Molecular Sieve Chromatography
Ion-Exchange Chromatography Procedure
Electrophoresis, Disc
Hydrogen-Ion Concentration
Plasma Protein Binding Capacity
Rice (Dietary)
Thiamine Mononitrate

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