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Apotransferrin proton dissociation and interactions with hydrogencarbonate in neutral media

โœ Scribed by Louisa Bellounis; Rowchanak Pakdaman; Jean Michel El Hage Chahine


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
594 KB
Volume
9
Category
Article
ISSN
0894-3230

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โœฆ Synopsis


A spectrofluorimetric titration analysis of the proton dissociation and the interactions of human serum transferrin with hydrogencarbonate was performed at pH 7-0-9.0. Apotransferrin loses a single proton probably per binding site with K , = (6.80i0.35) x M. This proton dissociation is independent of the hydrogencarbonate concentration. Apotransferrin does not interact with CO,'-. However, it interacts with two HCO,-, exhibiting two different affinity constants; the dissociation constant presumably for the C-site is K, = (4.4OrtO-15) x M and that for presumably the N-site is K , = (3.60i0.30) x lo-' M. These interactions


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