Protein with thiamine-binding activity (14 nmole/mg protein) was isolated from rat red cells by affinity chromatography. Adsorbents with varying degrees of hydrophoby containing thiamine as ligand were made use for isolation. A2300-fold purification with a 50% overall yield was attained. The protein preparation was found to be homogenous upon polyacrylamide gel electrophoresis. The role of pH of the medium, of ions of bivalent metals in vitamin B1 binding with the protein isolated has been shown.
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