Brunel University Research Archive (BURA) >
Schools >
School of Health Sciences and Social Care >
School of Health Sciences and Social Care Research Papers >

Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/4339

Title: Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-Terminal regions of the protein
Authors: Evans, RW
Williams, J
Publication Date: 1978
Publisher: Portland Press
Citation: Biochemical Journal 173: 543-552
Abstract: 1. Trypsin digestion of human serum transferrin partially saturated with iron(III)- nitrilotriacetate at pH5.5 or pH 8.5 produces a carbohydrate-containing iron-binding fragment of mol.wt. 43000. 2. When iron(III) citrate, FeCI3, iron(II) ascorbate and (NH4)2SO4,FeSO4 are used as iron donors to saturate the protein partially, at pH 8.5, proteolytic digestion yields a fragment of mol.wt. 36000 that lacks carbohydrate. 3. The two fragments differ in their antigenic structures, amino acid compositions and peptide 'maps'. 4. The fragment with mol.wt. 36000 was assigned to the N-terminal region of the protein and the other to the C-terminal region. 5. The distribution of iron in human serum transferrin partially saturated with various iron donors was examined by electrophoresis in urea/polyacrylamide gels and the two possible monoferric forms were unequivocally identified. 6. The site designated A on human serum transferrin [Harris (1977) Biochemistry 16, 560-564] was assigned to the C-terminal region of the protein and the B site to the N-terminal region. 7. The distribution of iron on transferrin in human plasma was determined.
URI: http://bura.brunel.ac.uk/handle/2438/4339
ISSN: 0264-6021
Appears in Collections:School of Health Sciences and Social Care Research Papers
Biological Sciences

Files in This Item:

File Description SizeFormat
biochemj-1978.pdf2.57 MBAdobe PDFView/Open

Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.