Isolation and characterization of riboflavin-binding protein from pregnant-rat serum.
A high-affinity riboflavin -binding protein was isolated and characterized for the first time from pregnant-rat sera by affinity chromatography on a lumiflavin-agarose column. The purified protein was homogeneous by the criteria of analytical polyacrylamide-gel disc electrophoresis, gel-filtration chromatography on Sephadex G-100 and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It had a molecular weight of 90000+/-5000 and interacted with [14C]riboflavin with a 1:1 molar ratio with a dissociation constant (Kd) of 0.42 micron.
D000818:Animals; D002352:Carrier Proteins / Q000097:blood*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008970:Molecular Weight; D011247:Pregnancy; D051381:Rats; D012256:Riboflavin / Q000097:blood*
D002352:Carrier Proteins; D012256:Riboflavin