| Literature DB >> 6673576 |
Abstract
A protein with thiamine-binding activity (14 nmole/mg protein) was isolated from rat red cells by affinity chromatography. Adsorbent with varying degrees of hydrophobicity containing thiamine as ligand were used for the isolation. A 2300-fold purification in a 50% overall yield was attained. The purified thiamine-binding protein is homogeneous on polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate.Entities:
Mesh:
Substances:
Year: 1983 PMID: 6673576
Source DB: PubMed Journal: Acta Vitaminol Enzymol ISSN: 0300-8924