Diagnosis of Hb M disease by electron paramagnetic resonance spectra.
1980
A Hayashi, and
T Suzuki, and
T Fujita
UI
MeSH Term
Description
Entries
D004578
Electron Spin Resonance Spectroscopy
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic
D006449
Hemoglobin M
A group of abnormal hemoglobins in which amino acid substitutions take place in either the alpha or beta chains but near the heme iron. This results in facilitated oxidation of the hemoglobin to yield excess methemoglobin which leads to cyanosis.
D006453
Hemoglobinopathies
A group of inherited disorders characterized by structural alterations within the hemoglobin molecule.
Hemoglobinopathy
D006455
Hemoglobins, Abnormal
Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains.
Abnormal Hemoglobins
D006801
Humans
Members of the species Homo sapiens.
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000596
Amino Acids
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.