DTSSP is a cross-linkingreagent reacting the amino groups with each other. Since DTSSP has at both ends of the molecule N-hydroxysuccinimide active ester to react selectively with the amino group, it can be conjugated a carrier protein to simple hapten or preparation labeled enzyme. BS3 takes a chemical structure having analkyl chain to the linker moiety. Meanwhile, DTSSP and DSP is capable of cleavage of the disulfide-introduced linker site that is easily reduced by the reducing agent. Further, since the active ester group having a sulfonic acid group is introduced to DTSSP and BS3, it may be carried out labeling reaction without using an organic solvent such as DMSO or DMF.
2. S. M. Jung and M. Moroi, “Crosslinking of Platelet Glycoprotein Ib by N-Succinimidyl(4-azidophenyldithio)propionateand 3,3′-Dithiobis(sulfosuccinimidyl propionate), Biochim. Biophys. Acta,1983, 761, 152.
3. C. L. Swaim, J. B. Smith and D. L. Smith, “Unexpected Products From theReaction of the Synthetic Cross-linker 3,3′-Dithiobis(sulfosuccinimidylpropionate), DTSSP with Peptides”, J. Am. Soc. Mass Spectrom., 2004,15, 736.
4. P. Kao, S. Doerner, T. Schneider, D. Allara, P. Hauptmann and S. Tadigadapa,”A Micromachined Quartz Resonator Array for Biosensing Applications”,J. Microekectromech. Syst., 2009, 18(3), 522.
5. G. J. King, A. Jones, B. Kobe, T. Huber, D. Mouradov, D. A. Hume and I. L.Ross, “Identification of Disulfide-containing Chemical Cross-links inProteins Using MALDI-TOF/TOF-Mass Spectrometry”, Anal. Chem., 2008,80, 5036.