Encyclopedia of Smart Materials (Vols 1 and 2) - M. Schwartz (2002) Episode 3

Tham khảo tài liệu 'encyclopedia of smart materials (vols 1 and 2) - m. schwartz (2002) episode 3', kỹ thuật - công nghệ, cơ khí - chế tạo máy phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Figure 13. Time course of the EOT neffZ of a p-type PSi chip etched at 440 mA cm2 oxidized by ozone for 20 min and functionalized as shown in Scheme 2 a. The arrow labeled A identifies the addition of 10 M streptavidin preincubated in 1 mM biotin dissolved in PBS buffer pH control B addition of 10 M streptavidin without biotin washing cycles in between C washing cycles with buffer D addition of dithiothreitol which was used to reduce the disulfide bridge and therefore release the bound protein-linker complex. The sample was mounted in a flow cell using a constant flow rate of mL min reprinted with permission from 59 . the silicon walls. Using an ethanol-water mixture instead of the protein solution results in a rectangular signal response upon adding the mixture and rinsing with water. Specific binding of streptavidin to the biotin-functionalized PSi matrix was measured by monitoring the changes in EOT time-resolved in a PBS buffer containing TritonTM to minimize nonspecific adsorption . binding sites were deactivated by saturati biotin in solution a change in EOT was not gesting that there is little or no nonspecific p tion to the PSi matrix. Rinsing the surface w the protein has bound does not alter the EO However because the biotin recognition ele to the surface via a disulfide bond the protei plex could be released from the surface by threitol to the bulk phase. The initial red upon binding streptavidin to the biotinylat completely reversed and provides further s interpretation that the observed red shift is binding of the protein to the functionalized over the reversible linkage of the protein bridges to the surface offers the possibility functionalized PSi chips for further bindin Sailor and co-workers bound protein A to t through the BSA-containing linker 60 61 binds to the biotin-terminated linker and ad sible free biotin-binding sites to the surface Adding a solution of biotinylated protei attaching it to the surface. This prefunction .

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