PROPERTIES OF STREPTAVIDIN BIOTIN-BINDING PROTEIN PRODUCED BY STREPTOMYCETES
PROPERTIES OF STREPTAVIDIN BIOTIN-BINDING PROTEIN PRODUCED BY STREPTOMYCETES
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DOI：
10.1016/0003-9861(64)90150-x
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发表时间：
1964-01-01
影响因子：
3.9
通讯作者：
WOLF, FJ
中科院分区：
文献类型：
--
作者：
CHAIET, L;WOLF, FJ
链霉亲和素是从链霉菌发酵滤液中分离得到的一种结晶蛋白，具有与亲和素类似的生物素结合能力。用微生物、物理和化学方法对蛋清中的链霉亲和素和亲和素进行了比较。链霉亲和素结合了四个生物素分子。化学分析表明，不存在与亲和素相关的己糖和氨基糖，并揭示了氨基酸含量的差异。电泳法研究表明，链霉亲和素和亲和素的迁移率不同。因此，链霉亲和素是一种新型的生物素结合蛋白。
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.