Interaction of Human Hemoglobin and Its Variants with Agar
- 8 July 1983
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 221 (4606), 175-178
- https://doi.org/10.1126/science.6190229
Abstract
In citrate agar electrophoresis hemoglobin appears to bind reversibly to the sulfated polysaccharide agaropectin, a natural component of Difco Bacto-Agar. This complex migrates anodally, since the hemoglobin is only weakly positively charged at pH 6.2 whereas the carbohydrate carries a net negative charge. Electroendosmosis, on the other hand, proceeds in the cathodal direction. These opposing fluxes separate the hemoglobins in the order of their affinity for agaropectin. An agaropectin binding site was identified on hemoglobin by computer-assisted modeling, and the relation of the site to hemoglobin variants that exhibit abnormal citrate agar mobility was established. The citrate anion is postulated to function as a "counter ion." Preliminary evidence indicates that agaropectin has antigelling properties with respect to hemoglobin S.This publication has 14 references indexed in Scilit:
- Correlation of mobilities of mutant hemoglobins in citrate agar electrophoresis with specific molecular locations of affected residuesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- A decreased effect of organic phosphates on hemoglobin S at low concentrationsBiochemical and Biophysical Research Communications, 1978
- Structure in Relation to Behavior of Mutant Hemoglobins in Citrate Agar ElectropiioresjsHemoglobin, 1977
- Effects of polyvalent anion binding to hemoglobin on oxygen and oxidation-reduction equilibria and their relevance to allosteric transitionJournal of Molecular Biology, 1975
- The agarose double helix and its function in agarose gel structureJournal of Molecular Biology, 1974
- Citrate Agar-gel Electrophoresis for Identifying Abnormal HemoglobinsAmerican Journal of Clinical Pathology, 1973
- Structure, Conformation, and Mechanism in the Formation of Polysaccharide Gels and NetworksPublished by Elsevier ,1969
- An improved method for preparing agaroseBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- Electrophoretic behaviour of haemoglobins in agar gelJournal of Chromatography A, 1961
- ON THE STRUCTURE OF AGAR FROM GELIDIUM CARTILAGINIUMCanadian Journal of Chemistry, 1956