Abstract
A specific protein exhibiting immunological cross-reactivity with chicken egg-white riboflavin carrier protein was detected by radioimmunoassay in the pregnancy sera of bonnet monkeys (Macaca radiata). This protein, which is capable of binding [14C]riboflavin, was purified by gel filtration on Sephacryl S-300, fast protein liquid chromatography on a Mono Q anion exchanger and chromatofocusing on Mono P columns. The isolated primate carrier protein was similar to its avian counterpart in terms of physicochemical characteristics, such as isoelectric point (pI ≤ 4), electrophoretic mobility, molecular weight (approx. 36000) and ligand binding. These findings may account for the extensive immunological cross-reactivity observed between the two proteins and suggest that the two vitamin carriers may have similar function in terms of embryonic vitamin nutrition.
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