Muniyappa, K and Adiga, PR (1980) Isolation and characterization of riboflavin-binding protein from pregnant-rat serum. In: Biochemical Journal, 187 (2). pp. 537-540.
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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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to the Biochemical Society.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||27 Aug 2009 05:25|
|Last Modified:||01 Mar 2012 06:38|
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