Oxidation of hemoglobin to methemoglobin in intact erythrocyte by a hydroperoxide induces formation of glutathionyl hemoglobin and binding of α-hemoglobin to membrane-Reference-Cited by-同舟云学术

Oxidation of hemoglobin to methemoglobin in intact erythrocyte by a hydroperoxide induces formation of glutathionyl hemoglobin and binding of α-hemoglobin to membrane

Published:2003-09 Issue:2 Volume:417 Page:244-250
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Murakami Kaori,Mawatari Shiro

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference36 articles.

1. Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin-hemoglobin cross-linking.

2. Effect of hemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins: correlation with a release of hemin

3. Oxidant damage of the lipids and proteins of the erythrocyte membranes in unstable hemoglobin disease. Evidence for the role of lipid peroxidation.

4. Red cell membrane remodeling in sickle cell anemia. Sequestration of membrane lipids and proteins in Heinz bodies.

5. Abnormal redox status of membrane-protein thiols in sickle erythrocytes.

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