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Structure and reactivity of hexacoordinate hemoglobins
Biophysical Chemistry, 2010 The heme prosthetic group in hemoglobins is most often attached to the globin through coordination of either one or two histidine side chains. Those proteins with one histidine coordinating the heme iron are called “pentacoordinate” hemoglobins, a group ...
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Spectrophotometry of Hemoglobin and Hemoglobin Derivatives
Advances in clinical chemistry, 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, W G, Zijlstra
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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
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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.
E P, Vichinsky, B H, Lubin
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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.
R W, Keane +3 more
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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.
A, Tomoda, Y, Yoneyama
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Biochemical Genetics, 1977
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.
G, Sterling, S T, Bowen
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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.
G, Sterling, S T, Bowen
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Critical Care Medicine, 2003
To review current knowledge about cell-free hemoglobin solutions.A computerized MEDLINE search was used to retrieve all studies concerning cell-free hemoglobin solutions from 1990 to 2003. The reference lists of all available review articles and primary studies were also reviewed to identify references not identified in the computerized search.All ...
Creteur, Jacques, Vincent, Jean Louis
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To review current knowledge about cell-free hemoglobin solutions.A computerized MEDLINE search was used to retrieve all studies concerning cell-free hemoglobin solutions from 1990 to 2003. The reference lists of all available review articles and primary studies were also reviewed to identify references not identified in the computerized search.All ...
Creteur, Jacques, Vincent, Jean Louis
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Xenopus laevis hemoglobin and its hybrids with hemoglobin A
Biochemistry, 1987Isolated alpha and beta chains from Xenopus laevis hemoglobin have been purified. The isolation procedure yields native alpha chains whose functional behavior has been characterized and compared with that of human alpha chains. Isolated beta chains in the presence of oxygen are characterized by low stability, and hence their functional characterization
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