Results 321 to 330 of about 902,120 (353)
Some of the next articles are maybe not open access.
2011
This chapter discusses in detail several aspects of hemoglobin’s function and its disorders. The chapter includes a description of mechanism of oxygen delivery by hemoglobin. Various clinical disorders such as various anemia, thalassemia syndromes, and sickle cell diseases are presented. A new method of treating hemoglobinopathies by reawakening of the
N.V. Bhagavan, Chung-Eun Ha
openaire +4 more sources
This chapter discusses in detail several aspects of hemoglobin’s function and its disorders. The chapter includes a description of mechanism of oxygen delivery by hemoglobin. Various clinical disorders such as various anemia, thalassemia syndromes, and sickle cell diseases are presented. A new method of treating hemoglobinopathies by reawakening of the
N.V. Bhagavan, Chung-Eun Ha
openaire +4 more sources
Spectrophotometry of Hemoglobin and Hemoglobin Derivatives
1983Publisher Summary This chapter presents a discussion of spectrophotometry of hemoglobin and hemoglobin derivatives. Many special photometers (hemoglobinometers, oximeters, etc.) presently available for the determination of hemoglobin and hemoglobin derivatives are mentioned only incidentally.
E.J. Van Kampen, Willem G. Zijlstra
openaire +2 more sources
The organization of hemoglobin in erythrocytes containing hemoglobin A or hemoglobin C
Canadian Journal of Physiology and Pharmacology, 1970Red cells containing hemoglobin C have been shown to behave as if they are more rigid than normal cells that contain hemoglobin A. Under some conditions the former cells contain inclusions that appear to be crystalline. This study shows, by X-ray scattering and diffraction, that the inclusions are crystalline.
R. P. Rand, S. Charache
openaire +3 more sources
Ontogeny of hemoglobins: Evidence for hemoglobin M
Developmental Biology, 1974Abstract A new autosomal codominant hemoglobin mutation alters hemoglobin M of the primitive red cell line and hemoglobin D found in definitive cells. That Hb M and Hb D are altered by the same gene mutation supports the idea that Hb M shares a polypeptide chain with Hb D.
Vernon M. Ingram+3 more
openaire +3 more sources
Unstable Hemoglobins, Hemoglobins with Altered Oxygen Affinity, and M-Hemoglobins
Pediatric Clinics of North America, 1980Most patients with chronic Heinz body anemia do not require treatment. Dietary folic acid supplementation is recommended when hemolysis is chronic and severe. During infection, patients should be observed carefully because of the possibility of aplastic or hemolytic crises.
Elliott Vichinsky, Bertram H. Lubin
openaire +3 more sources
OBSERVATIONS ON HEMOGLOBIN "PYLOS": THE HEMOGLOBIN PYLOS-HEMOGLOBIN S COMBINATION.
The Journal of laboratory and clinical medicine, 1963Abstract Two cases, the first reported in the medical literature, of association of the hemoglobin "Pylos" anomaly and hemoglobin S are discussed. The clinical picture and laboratory findings are presented, and the difficulty of accurate diagnosis by the routine procedures of hemoglobin analysis is emphasized. The findings are discussed in relation to
Phaedon Fessas, G. Stamatoyannopoulos
openaire +3 more sources
The hemoglobins of Artemia salina. V. Genetic variation in hemoglobin 1, hemoglobin 2, and hemoglobin 3 [PDF]
Electrophoretic mobilities of three hemoglobins (Hb1, Hb2, and Hb3) were studied in 15 populations of brine shrimps. Genetic segregation data support the model that Hb2 contains n alpha-polypeptides and n beta-polypeptides; Hb1 contains 2n alpha-polypeptides- Hb3 contains neither alpha- nor beta-polypeptides.
Gery Sterling, Sarane T. Bowen
openaire +2 more sources
On the relationship of hemoglobin oxidation with the conformation of hemoglobin
Experientia, 1979The rate of hemoglobin oxidation by various oxidants was studied under aerobic and anaerobic conditions, and the mechanism of hemoglobin oxidation was discussed in relation to the conformation of hemoglobin.
Akio Tomoda, Yoshimasa Yoneyama
openaire +3 more sources
Archives of Biochemistry and Biophysics, 1977
Abstract Transverse water proton relaxation times ( T 2 ) have been measured as a function of time after deoxygenation of solutions containing hemoglobin S. The shortened T 2 values observed upon deoxygenation of hemoglobin S result from an increase in the correlation time ( τ c ) of the water fraction irrotationally bound to deoxyhemoglobin S ...
Waterman Mr+5 more
openaire +3 more sources
Abstract Transverse water proton relaxation times ( T 2 ) have been measured as a function of time after deoxygenation of solutions containing hemoglobin S. The shortened T 2 values observed upon deoxygenation of hemoglobin S result from an increase in the correlation time ( τ c ) of the water fraction irrotationally bound to deoxyhemoglobin S ...
Waterman Mr+5 more
openaire +3 more sources