Abstract
Streptavidin, a crystalline protein isolated from fermentation filtrates of streptomycetes has been reported to have biotin-binding ability similar to avidin. A comparison has been made between streptavidin and avidin from egg white using microbiological, physical, and chemical methods. Streptavidin binds four molecules of biotin. Chemical analysis shows the absence of hexoses and amino sugars associated with avidin and reveals differences in amino acid content. Electrophoretic studies give different mobilities for streptavidin and avidin. Thus, streptavidin is a new type of biotin-binding protein.
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