Mechanism of Iron Removal From Transferrin

Harris, Wesley R.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
• Type: Research Project (R01)
• Project #: 5R01DK035533-11
• Application #: 2139592
• Study Section: Metallobiochemistry Study Section (BMT)
• Project Start: 1984-08-06
• Project End: 1998-04-30
• Budget Start: 1996-05-01
• Budget End: 1998-04-30
• Support Year: 11
• Fiscal Year: 1996

Institution

• Name: University of Missouri-St. Louis
• Department: Chemistry
• Type: Schools of Arts and Sciences
• City: Saint Louis
• State: MO
• Country: United States
• Zip Code: 63121

Publications

Bewley, M C; Tam, B M; Grewal, J et al. (1999) X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry 38:2535-41

Harris, W R; Yang, B; Abdollahi, S et al. (1999) Steric restrictions on the binding of large metal ions to serum transferrin. J Inorg Biochem 76:231-42

Li, Y; Harris, W R (1998) Iron removal from monoferric human serum transferrins by 1, 2-dimethyl-3-hydroxypyridin-4-one, 1-hydroxypyridin-2-one and acetohydroxamic acid. Biochim Biophys Acta 1387:89-102

MacGillivray, R T; Moore, S A; Chen, J et al. (1998) Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry 37:7919-28