BIOMAT Database Logo BIOMAT Database Logo

Kinetics of polymerization of deoxyhemoglobin S and mixtures of hemoglobin A and hemoglobin S at high hemoglobin concentrations. 1977

G L Cottam, and M R Waterman, and B C Thompson

UI MeSH Term Description Entries
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010100 Oxygen An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. Dioxygen,Oxygen-16,Oxygen 16
D011108 Polymers Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS). Polymer
D006441 Hemoglobin A Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.
D006451 Hemoglobin, Sickle An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia. Hemoglobin S,Deoxygenated Sickle Hemoglobin,Deoxyhemoglobin S,Hemoglobin SS,Hemoglobin, Deoxygenated Sickle,SS, Hemoglobin,Sickle Hemoglobin,Sickle Hemoglobin, Deoxygenated
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

G L Cottam, and M R Waterman, and B C Thompson
Polymerization of binary mixtures of hemoglobin S and carbamylated hemoglobin S.
January 1984, The Journal of biological chemistry,
G L Cottam, and M R Waterman, and B C Thompson
Aggregation of deoxyhemoglobin S at low concentrations.
December 1976, The Journal of biological chemistry,
G L Cottam, and M R Waterman, and B C Thompson
Inhibition of deoxyhemoglobin S polymerization by biaromatic peptides found to associate with the hemoglobin molecule at a preferred site.
April 1985, Biochemistry,
G L Cottam, and M R Waterman, and B C Thompson
Viscometric and spectrophotometric measurements of hemoglobin S polymerization kinetics.
April 1984, Blood,
G L Cottam, and M R Waterman, and B C Thompson
Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde.
January 1984, Analytical biochemistry,
G L Cottam, and M R Waterman, and B C Thompson
Polymerization of carbamylated deoxyhemoglobin S in concentrated phosphate buffer.
November 1982, The Journal of biological chemistry,
G L Cottam, and M R Waterman, and B C Thompson
Nucleation-controlled aggregation of deoxyhemoglobin S. Participation of hemoglobin A in the aggregation of deoxyhemoglobin S in concentrated phosphate buffer.
April 1980, The Journal of biological chemistry,
G L Cottam, and M R Waterman, and B C Thompson
Ionic strength dependence of the polymer solubilities of deoxyhemoglobin S + C and S + A mixtures.
April 1986, Blood,
G L Cottam, and M R Waterman, and B C Thompson
Kinetics of polymerization of hemoglobin S modified by thiol reagents and by oxidation.
July 1985, Biochimica et biophysica acta,
G L Cottam, and M R Waterman, and B C Thompson
Effect of the beta 73 amino acid on the hydrophobicity, solubility, and the kinetics of polymerization of deoxyhemoglobin S.
August 1987, The Journal of biological chemistry,
Copied contents to your clipboard!