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

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.

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 Creators:
Kampmann, Lutz1, Author           
Lepke, Sigrid1, Author           
Passow, Hermann1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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Free keywords: red cell membrane; band 3 protein; anion transport; 2DIDS 4,4'-diisothiocyanato dihydrostilbene-2,2'-disulfonic acid
 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.

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Language(s): eng - English
 Dates: 2014-06-271982-05
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Protides of the Biological Fluids
Source Genre: Series
 Creator(s):
Peeters, H., Editor
Affiliations:
-
Publ. Info: Oxford and New York : Pergamon Press
Pages: 984 Volume / Issue: 29 Sequence Number: - Start / End Page: 275 - 278 Identifier: ISBN: 978-0-08-027988-6
ISSN: 0079-7065