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. 1980 May 1;187(2):537–540. doi: 10.1042/bj1870537

Isolation and characterization of riboflavin-binding protein from pregnant-rat serum.

K Muniyappa, P R Adiga
PMCID: PMC1161823  PMID: 7396861

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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