Chapter title |
The Penultimate Tyrosine Residues are Critical for the Genotoxic Effect of Human Hemoglobin
|
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Chapter number | 46 |
Book title |
Oxygen Transport to Tissue XXXIX
|
Published in |
Advances in experimental medicine and biology, July 2017
|
DOI | 10.1007/978-3-319-55231-6_46 |
Pubmed ID | |
Book ISBNs |
978-3-31-955229-3, 978-3-31-955231-6
|
Authors |
Sandeep Chakane, Vijay Markad, Kisan Kodam, Leif Bülow |
Abstract |
Hemoglobin (Hb) is a potent oxidant outside the erythrocyte. The tyrosines α140 and β145 play an important role in the structure and function of Hb by forming switch and hinge contacts. These carboxy-terminal residues of the alpha and beta chains, respectively, were replaced to phenylalanine and several different methods were used to characterize the obtained mutants including a comet and plasmid DNA cleavage assay. It was observed that the genotoxic effect was 40% higher for αY140F compared with the wildtype, the βY145F and the double (αY140/β145F) mutants as determined by the comet assay. Cleavage of purified plasmid DNA after Hb application also revealed that the αY140F mutant showed 2-fold higher activity, while the βY145F and αY140/β145F mutants reduced the activity compared to wildtype Hb. This study clearly indicates that the penultimate tyrosines are involved in the genotoxicity of Hb. |
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