Homoglobin Rouen (α-140 (HC2) Tyr→His): alteration of the α-chain C-terminal region and moderate increase in oxygen affinity
| Autor: | Michael C. Marden, Jean Kister, Frédéric Galactéros, Henri Wajcman, M. Monconduit, A. Lahary |
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| Rok vydání: | 1992 |
| Předmět: |
Male
medicine.medical_specialty Stereochemistry Hemoglobins Abnormal Allosteric regulation Cooperativity Oxygen affinity Polycythemia vera Allosteric Regulation Internal medicine medicine Humans Histidine Amino Acids Polycythemia Vera Molecular Biology Chromatography High Pressure Liquid Aged Aged 80 and over Carbon Monoxide Chemistry Serine Endopeptidases medicine.disease Oxygen Kinetics Endocrinology Mutation Tyrosine Molecular Medicine Hemoglobin |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1180:53-57 |
| ISSN: | 0925-4439 |
| DOI: | 10.1016/0925-4439(92)90026-j |
| Popis: | Hb Rouen (alpha 140(HC2) Tyr--His) is a moderately high oxygen-affinity variant that was found in coincidence with polycythemia vera in a French patient. This hemoglobin provides an example of an alteration of the C-terminus of the alpha-chain, a region involved in the mechanisms of allosteric regulation. The increase in oxygen-affinity and decrease in cooperativity of this variant is much smaller than that resulting from the same substitution in the beta-chain. This model provides additional evidence for the inequivalence between the alpha- and beta-subunits. |
| Databáze: | OpenAIRE |
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