Allosterich properties of hemoglobin and the plasma membrane of the erythrocyte: New insights in Gas Transport and Metabolic Modulation
| Autor: | Bruno Giardina, Antonio Galtieri, Cristiana Carelli Alinovi, Maria Cristina De Rosa, Antonio Russo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Blood Glucose
Macromolecular Substances Clinical Biochemistry Allosteric regulation Oxidative phosphorylation Biochemistry band 3 Diffusion Hemoglobins Allosteric Regulation nitric oxide Anion Exchange Protein 1 Erythrocyte Genetics medicine Humans Molecular Biology Band 3 Settore BIO/10 - BIOCHIMICA red blood cells 2 3-DPG glycolysis 2 3-Diphosphoglycerate S-Nitrosothiols biology Chemistry Erythrocyte Membrane Oxygen transport Cell Biology Red blood cell medicine.anatomical_structure Membrane biology.protein Hemoglobin Gases Glycolysis Oxidation-Reduction 2 3-DPG Function (biology) |
| Zdroj: | IUBMB life 60 (2008): 87–93. info:cnr-pdr/source/autori:Maria Cristina De Rosa; Cristiana Carelli Alinovi; Antonio Galtieri; Annamaria Russo; Bruno Giardina/titolo:Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: New insights in gas transport and metabolic modulation/doi:/rivista:IUBMB life (Print)/anno:2008/pagina_da:87/pagina_a:93/intervallo_pagine:87–93/volume:60 |
| Popis: | Within the red blood cell the hemoglobin molecule is subjected to modulation mechanisms, namely homo- and heterotropic interactions, which optimize its functional behavior to the specific physiological requirements. At the cellular level, these modulation mechanisms are utilized to perform a number of other functions that are not minor with respect to the basic function of oxygen transport. Here we report some key examples concerning: (i) the interaction of hemoglobin with band 3 and its influence on glucose metabolism; (ii) the role of the ligand-linked quaternary transition of hemoglobin in the control of ''NO bioactivity'' and of gas diffusion; (iii) the interaction of plasma membrane with the various oxidative derivatives of the hemoglobin molecule. |
| Databáze: | OpenAIRE |
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