Thiamine-binding protein from rat erythrocytes

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.