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Au-BSA

Fig. 12 Fluorescent microscopic images showing interaction of Au-BSA-FA NCs with different types of cell lines (al-a2) FR-ve lung carcinoma A549 after 2 h of incubation, (bl-b2) FR-ve lung carcinoma A549 after 24 h of incubation, (cl-c2) FR+ve KB cells with unconjugated Au clusters, (dl-d2) FR+ve KB cells with FA conjugated Au clusters at 2 h, (el-e2) 4 h and (fl-f2) 24 h of incubation[25]... Fig. 12 Fluorescent microscopic images showing interaction of Au-BSA-FA NCs with different types of cell lines (al-a2) FR-ve lung carcinoma A549 after 2 h of incubation, (bl-b2) FR-ve lung carcinoma A549 after 24 h of incubation, (cl-c2) FR+ve KB cells with unconjugated Au clusters, (dl-d2) FR+ve KB cells with FA conjugated Au clusters at 2 h, (el-e2) 4 h and (fl-f2) 24 h of incubation[25]...
Au-BSA-Ag Ab-HRP Amperometry Clenbuterol in TMB/HjOj solution Livestock urine Competitive assay Sixteen electrodes [55]... [Pg.239]

Hu, C., D.-P. Yang, Z. Wang, L. Yu, J. Zhang, and N. Jia. 2013. Improved FIS performance of an electrochemical cytosensor using three-dimensional architecture Au BSA as sensing layer. Anal. Chem. 85 5200-5206. [Pg.505]

Tris-HCl (120 gL), CaCl2 (60 gL), BSA (60 gL), DTT (3 gL), water (87 /iL) and freshly thawed microsomal fraction (30 gL) were mixed well and divided into three reaction tubes one reaction and two control tubes (1 and 2). 40 uL of freshly prepared UDPGA was added to the reaction tube and control 1 and 40 yfL of water to the control 2. The tubes were pre-incubated for 2 min in a water bath shaker at 35 °C. Then, 20 yiL of freshly prepared solutions of substrate in 20 % DMSO was added to the reaction and control 2 tubes, as well as 20 /rL of water to the control 1 mbe. Aliquots of 50 /rL were withdrawn from aU tubes and were quenched in acidified ice-cold methanol (160 gL per each 50 gL aliquot). The quenched aliquots collected during the incubation were left on ice for at least 20 min. After centrifugation for 10 min at 12000 rpm, the supernatants were collected into glass mbes and the remaining proteinaceous pellets were washed twice with 50 /iL of water and reprecipitated with 150 /iL of ice-cold methanol. The combined supernatants were dried under N2 gas and reconstimted into 50 /iL of appropriate mobile phase. [Pg.247]

Immerse the slide in 1 M ethanolamine solution, 3% BSA (pH 8.5) for blocking nonspotted surface of Au-coated slide and masking the nonreacted succinimide esters at 25°C for 30 min. [Pg.220]

Transverse IEF was also conducted in a pressure-driven flow for BSA and soybean lectin separation on-chip [1040], Here, Pd electrodes were used (in preference to Au) because of the non-gassing character of Pd. In addition, the protein sample was sandwiched between two buffer streams and was prevented from direct contact with the channel wall (and hence the electrode), a process akin to hydrodynamic focusing [1040],... [Pg.352]

Figure 9. Schematic fabrication of LbL films comprising poly(vinylsulfonic acid) (PVS)and PAMAM-Au. The sequential deposition of LbL multilayers was carried out by immersing the substrate alternately into (a) PVS and (b) PAMAM-Au solutions for 5 min per step (c) After deposition of 3 bilayers, an ITO-PVS/PAMAM-Au)3 CoHCF electrode was prepared by potential cycling (d) The enzyme immobilization to produce ITO-PVS/PAMAM-Au)3 CoHCF-GOx was carried out in a solution containing BSA, glutaraldehyde and GOx (Adapted from Ref.[124])... Figure 9. Schematic fabrication of LbL films comprising poly(vinylsulfonic acid) (PVS)and PAMAM-Au. The sequential deposition of LbL multilayers was carried out by immersing the substrate alternately into (a) PVS and (b) PAMAM-Au solutions for 5 min per step (c) After deposition of 3 bilayers, an ITO-PVS/PAMAM-Au)3 CoHCF electrode was prepared by potential cycling (d) The enzyme immobilization to produce ITO-PVS/PAMAM-Au)3 CoHCF-GOx was carried out in a solution containing BSA, glutaraldehyde and GOx (Adapted from Ref.[124])...
Fig. 10 Subsequent additions of biotin-BSA (i), lipid vesicles (ii), NeutrAvidin (in), single-stranded biotin-DNA (iv), and lipid vesicles modified with fully complementary DNA (v) to a Si02-coated and b Au-coated QCM crystals. Note that there is no adsorption of biotin-BSA on Si02, while the efficient binding of biotin-BSA on An significantly reduces vesicles adsorption to the Au-coated surface. Similarly, the bilayer formation renders the Si02-coated surface inert to subsequent additions of DNA and vesicles. The micrograph shows sequence-specific sorting of two differently fluorescently labeled DNA-modified vesicles to spots modified with different DNA sequences... Fig. 10 Subsequent additions of biotin-BSA (i), lipid vesicles (ii), NeutrAvidin (in), single-stranded biotin-DNA (iv), and lipid vesicles modified with fully complementary DNA (v) to a Si02-coated and b Au-coated QCM crystals. Note that there is no adsorption of biotin-BSA on Si02, while the efficient binding of biotin-BSA on An significantly reduces vesicles adsorption to the Au-coated surface. Similarly, the bilayer formation renders the Si02-coated surface inert to subsequent additions of DNA and vesicles. The micrograph shows sequence-specific sorting of two differently fluorescently labeled DNA-modified vesicles to spots modified with different DNA sequences...
Scheme 1 Schematic representation of protein protected cluster formation taking BSA as an example. The reaction proceeds via formation of Au -protein intermediate adduct. After cluster formation intense red luminescence is observed under UV light. Scheme 1 Schematic representation of protein protected cluster formation taking BSA as an example. The reaction proceeds via formation of Au -protein intermediate adduct. After cluster formation intense red luminescence is observed under UV light.
Fig. 11 (A) MALDI MS of AU4, Aug and Auio protected with BSA synthesized at pH 7.4 (using phosphate buffer) by varying BSA to Au ratio from 1 5,1 8 and 1 12, respectively. Aui3 and AU25 are shown in (B). AU]3 was prepared at pH 7.4 using BSA Au ratio to be 1 24 while Au25 was prepared at pH 11. Reproduced from Ref. 152 with permission from The Royal Society of Chemistry. Fig. 11 (A) MALDI MS of AU4, Aug and Auio protected with BSA synthesized at pH 7.4 (using phosphate buffer) by varying BSA to Au ratio from 1 5,1 8 and 1 12, respectively. Aui3 and AU25 are shown in (B). AU]3 was prepared at pH 7.4 using BSA Au ratio to be 1 24 while Au25 was prepared at pH 11. Reproduced from Ref. 152 with permission from The Royal Society of Chemistry.

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