Cite
Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-arm Exchange.
MLA
Bremer, Ewald T. J.van den, et al. “Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-Arm Exchange.” Analytical Chemistry, vol. 89, no. 20, Oct. 2017, pp. 10873–82. EBSCOhost, https://doi.org/10.1021/acs.analchem.7b02543.
APA
Bremer, E. T. J. van den, Labrijn, A. F., van den Boogaard, R., Priem, P., Scheffler, K., Melis, J. P. M., Schuurman, J., Parren, P. W. H. I., & Jong, R. N. de. (2017). Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-arm Exchange. Analytical Chemistry, 89(20), 10873–10882. https://doi.org/10.1021/acs.analchem.7b02543
Chicago
Bremer, Ewald T. J. van den, Aran F. Labrijn, Ramon van den Boogaard, Patrick Priem, Kai Scheffler, Joost P. M. Melis, Janine Schuurman, Paul W. H. I. Parren, and Rob N. de Jong. 2017. “Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-Arm Exchange.” Analytical Chemistry 89 (20): 10873–82. doi:10.1021/acs.analchem.7b02543.