Identification and characterization of riboflavin-binding proteins in human circulation
Riboflavin binding by plasma proteins from healthy human subjects was examined by equilibrium dialysis and binding was observed to vary over a greater than 10-fold range. Upon fractionation of plasma by gel filtration, the major riboflavin-binding components eluted with albumin and gamma-globulins. Albumin was purified and found to bind riboflavin only very weakly, although FMN and photo-chemical degradation products were more tightly bound. Most of the binding occurred in the gamma-globulin fraction and was attributed to immunoglobulins because the binding proteins and immunoglobulins copurified using various methods, were removed by treatment of plasma with protein A-agarose, and were coincident upon immuno-electrophoresis followed by autoradiography to detect (2-{sup 14}C)-riboflavin. Binding differences among plasma samples were reflected in the binding recovered with the immunoglobulin fractions; however, there was not a direct relationship between the amount of immunoglobulin and the amount of (2-{sup 14}C)riboflavin bound. Hence, it appeared that the binding was due to a subfraction of immunoglobulins.
- Research Organization:
- Emory Univ., Atlanta, GA (USA)
- OSTI ID:
- 5406699
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PROTEINS
CHEMICAL COMPOSITION
RIBOFLAVIN
BIOCHEMICAL REACTION KINETICS
ALBUMINS
AUTORADIOGRAPHY
CARBON 14 COMPOUNDS
ELECTROPHORESIS
GLOBULINS
IMMUNOGLOBULINS
MAN
ANIMALS
KINETICS
LABELLED COMPOUNDS
MAMMALS
ORGANIC COMPOUNDS
PRIMATES
REACTION KINETICS
VERTEBRATES
VITAMIN B GROUP
VITAMINS
550201* - Biochemistry- Tracer Techniques