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The Kinetics of Intramolecular Crosslinking of the Band 3 Protein by 4,4'-Diisothiocyanato Dihydrostilbene-2,2'-Disulfonic Acid (H2Dids)

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Kampmann,  Lutz
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Lepke,  Sigrid
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Passow,  Hermann
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kampmann, L., Lepke, S., & Passow, H. (1982). The Kinetics of Intramolecular Crosslinking of the Band 3 Protein by 4,4'-Diisothiocyanato Dihydrostilbene-2,2'-Disulfonic Acid (H2Dids). In H. Peeters (Ed.), Protides of the Biological Fluids (pp. 275-278). Oxford and New York: Pergamon Press. doi:10.1016/B978-0-08-027988-6.50065-3.


Cite as: http://hdl.handle.net/21.11116/0000-0007-DE2B-0
Abstract
The time course of intramolecular crosslinking by H2DIDS of two lysine residues called lys a and lys b on the chymotryptic 60k and 35k dalton segments, respectively, of the band 3 protein is described. One of the two isothiocyanate groups of the H2DIDS molecule may react first either with lys a or lys b. In a subsequent step the crosslink is established by a reaction of the other isothiocyanate group with lys b or lys a, respectively. The mathematical analysis of the data shows that the reaction rate with lys a is 2 to 3.5 times higher than the reaction rate with lys b. The establishment of the crosslink by H2DIDS molecules that are unilaterally bound to either lys a or lys b takes place at a rate that is about one order of magnitude lower than the rate of establishment of the unilateral bond. A more detailed analysis of the data suggests that the H2DIDS binding site may exist in two different conformational states in which lys a is either more susceptible or less susceptible to covalent bond formation with H2DIDS.