Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release
Publication
, Journal Article
Dhungana, S; Crumbliss, AL
Published in: Chemtracts
December 1, 2000
Desired mutations were successfully introduced to the N-lobe of human transferrin in which Glu, Gln, and Ala replaced His 249. The structural analysis of H249E mutant was successfully carried out and was compared with the wild type. The pH stability of the mutants and the kinetic stability of the Fe-mutant complexes were determined and were found to be in accordance with similar investigations carried out in the past.
Duke Scholars
Published In
Chemtracts
ISSN
1431-9268
Publication Date
December 1, 2000
Volume
13
Issue
12
Start / End Page
770 / 775
Related Subject Headings
- Organic Chemistry
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Dhungana, S., & Crumbliss, A. L. (2000). Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release. Chemtracts, 13(12), 770–775.
Dhungana, S., and A. L. Crumbliss. “Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release.” Chemtracts 13, no. 12 (December 1, 2000): 770–75.
Dhungana S, Crumbliss AL. Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release. Chemtracts. 2000 Dec 1;13(12):770–5.
Dhungana, S., and A. L. Crumbliss. “Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release.” Chemtracts, vol. 13, no. 12, Dec. 2000, pp. 770–75.
Dhungana S, Crumbliss AL. Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release. Chemtracts. 2000 Dec 1;13(12):770–775.
Published In
Chemtracts
ISSN
1431-9268
Publication Date
December 1, 2000
Volume
13
Issue
12
Start / End Page
770 / 775
Related Subject Headings
- Organic Chemistry