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Alteration of infrared spectrum of serum transferrin by iron binding and lowered pH

✍ Scribed by Robert J. Donohoe

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 84 KB
Volume: 5
Category: Article
ISSN: 1075-4261
DOI: 10.1002/(sici)1520-6343(1999)5:6<325::aid-bspy1>3.0.co;2-p

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✦ Synopsis

Difference infrared spectra are reported for human serum transferrin in D2O as a function of iron binding or increased acidity. Spectral features detected as iron is bound at high pH include difference bands that are indicative of reduced solvent exposure and binding site ligation. More extensive spectral alterations, some of which indicate titration of carboxylic acid groups, are induced in the apo protein by lowering the pH in a manner consistent with that entailed in endocytosis.

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## Abstract Transferrin (TF) is a bilobal transport protein that acquires ferric iron from the diet and holds it tightly within the cleft of each lobe (thereby preventing its hydrolysis). The iron is delivered to actively dividing cells by receptor mediated endocytosis in which diferric TF preferen