| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7753659 | Journal of Inorganic Biochemistry | 2018 | 8 Pages |
Abstract
The glycation site specificity of human diferric holo-transferrin (Tf) was evaluated using tandem mass spectrometry. The glycation pattern was different from apo-Tf, with lysine residues 103, 312 and 380 proving to be the most reactive sites in holo-Tf. An in silico approach evaluated the role of the lysine microenvironment.197
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
André M.N. Silva, João T.S. Coimbra, Maria M. Castro, Ãngela Oliveira, Natércia F. Brás, Pedro A. Fernandes, Maria J. Ramos, Maria Rangel,