Biomaterial Database

Determination of the amounts and oxidation states of hemoglobins M Boston and M Saskatoon in single erythrocytes by infrared microspectroscopy. 1994

A Dong, and M Nagai, and Y Yoneyama, and W S Caughey

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523.

The reduced abnormal subunits of two M-type hemoglobins, Boston (His alpha 58-->Tyr) and Saskatoon (His beta 63-->Tyr), have been determined in the presence of normal human hemoglobin A by measurement of C-O stretch bands in infrared spectra of carbon monoxide complexes. Use of an infrared microscope coupled to a Fourier transform infrared spectrometer of high sensitivity permitted measurements to be made on as small a hemoglobin mixture as is contained in a single erythrocyte. The abnormal subunits of both Hbs M exhibit bands near 1970 cm-1 compared with bands near 1951 cm-1 for the normal subunits. The increase in 1970 cm-1 band intensity upon erythrocyte reduction with dithionite provided a measure of the extent of abnormal subunit oxidation; in cell suspensions about 60% of the abnormal subunits of Hb M Boston and 80% for Hb M Saskatoon remained reduced. The amount of Hb present as abnormal Hb averaged about 25% for Hb M Boston cells and about 50% for Hb M Saskatoon cells. However, the ratio of Hb M to Hb A in individual cells varied markedly, with the ratio expected to decrease as the cell ages. These results demonstrate the unique utility of infrared microspectroscopy for the study of differences in abnormal Hb status among individual erythrocytes.

UI	MeSH Term	Description	Entries
D008853	Microscopy	The use of instrumentation and techniques for visualizing material and details that cannot be seen by the unaided eye. It is usually done by enlarging images, transmitted by light or electron beams, with optical or magnetic lenses that magnify the entire image field. With scanning microscopy, images are generated by collecting output from the specimen in a point-by-point fashion, on a magnified scale, as it is scanned by a narrow beam of light or electrons, a laser, a conductive probe, or a topographical probe.	Compound Microscopy,Hand-Held Microscopy,Light Microscopy,Optical Microscopy,Simple Microscopy,Hand Held Microscopy,Microscopy, Compound,Microscopy, Hand-Held,Microscopy, Light,Microscopy, Optical,Microscopy, Simple
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D002263	Carboxyhemoglobin		Carbomonoxyhemoglobin,Carbonmonoxyhemoglobin,Carbonylhemoglobin,Carboxyhemoglobin A,Carboxyhemoglobin C
D004912	Erythrocytes	Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.	Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D005583	Fourier Analysis	Analysis based on the mathematical function first formulated by Jean-Baptiste-Joseph Fourier in 1807. The function, known as the Fourier transform, describes the sinusoidal pattern of any fluctuating pattern in the physical world in terms of its amplitude and its phase. It has broad applications in biomedicine, e.g., analysis of the x-ray crystallography data pivotal in identifying the double helical nature of DNA and in analysis of other molecules, including viruses, and the modified back-projection algorithm universally used in computerized tomography imaging, etc. (From Segen, The Dictionary of Modern Medicine, 1992)	Fourier Series,Fourier Transform,Analysis, Cyclic,Analysis, Fourier,Cyclic Analysis,Analyses, Cyclic,Cyclic Analyses,Series, Fourier,Transform, Fourier
D006441	Hemoglobin A	Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.
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