Abstract
The strong binding between streptavidin (SA) and biotin has been used as a useful tool in the study of biological system. When SA is mixed with biotinylated bovine serum albumin (bBSA), aggregates are formed by crosslinking. We employed fluorescence correlation spectroscopy to determine the hydrodynamic radius of SA‐bBSA aggregates. We found that their hydrodynamic radius depends on the molar ratio of SA to bBSA, with the maximum radius being observed for 4:1 SA to bBSA. When the molar ratio of SA to bBSA was 6:1, the size of the aggregates decreased sharply because the SA molecules surround the bBSA and as a result, crosslinking is greatly reduced. Based on the hydration radius of the aggregates, we estimate that 7 to 8 SA molecules were bound to one bBSA.
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