نتایج جستجو برای: hemoglobins

تعداد نتایج: 1615  

Journal: :The Journal of General Physiology 1941
Kurt Salomon

1. Two high molecular invertebrate hemoglobins (the erythrocruorins of Lumbricus terrestris and of Nereis virens) as well as the low molecular erythrocruorin of Glycera dibranchiata Ehlers were studied. Their physical chemical properties were compared with those of vertebrate hemoglobin. 2. The hemin of the blood pigment of Glycera dibranchiata Ehlers was shown to be identical with that of vert...

Journal: :Blood 1976
R G Schneider B Hightower T S Hosty H Ryder G Tomlin R Atkins B Brimhall R T Jones

Hemolysates of erythrocytes from more than a quarter million people in Alabama were electrophoresed on cellulose acetate, pH 8.4, and those samples exhibiting an abnormality were also electrophoresed in citrate agar, pH 6.0. The globin chains of mutants other than Hb S and C were electrophoresed in urea-mercaptoethanol buffers at both pH 8.9 and pH 6.0, and 60 of them were also analyzed structu...

Journal: :Blood 1969
R L Nagel H M Ranney T B Bradley A Jacobs L Udem

T HE ASSOCIATION of congenital nonspherocytic hemolytic anemia with the presence of certain unstable hemoglobins has been recognized in numerous patients.1 The instability of these hemoglobins has been manifested by precipitation on heating in vitro and by the formation of Heinz bodies with premature destruction of erythrocytes in vivo. The molecular basis for the instability of certain of thes...

Journal: :The Journal of experimental biology 2007
Jonathan B Wittenberg Beatrice A Wittenberg

The heart, red skeletal muscles and the nitrogen-fixing legume root nodule function in steady states of high oxygen influx, partial oxygenation of cytoplasmic myoglobin or leghemoglobin and correspondingly low oxygen partial pressure. Here, we ask: what conditions are required at the surface of actively respiring, state III, tightly coupled mitochondria to enhance oxygen flow to cytochrome oxid...

Journal: :Clinical chemistry 1983
R G Ryall C J Story

Hemoglobin-oxygen association curves of human erythrocytes were measured in metabolically stable cells under the standardized conditions of extracellular pH 7.400, carbon dioxide tension 38 mmHg (approximately 5 kPa) and temperature 37 degrees C. A model of the oxygen association curve of normal erythrocytes was subsequently developed, based on assumed equilibrium reactions between hemoglobins ...

Journal: :Comparative biochemistry and physiology. Part A, Molecular & integrative physiology 2010
Cédric Meunier Ann C Andersen Matthieu Bruneaux Dominique Le Guen Peran Terrier Emmanuelle Leize-Wagner Franck Zal

Siboglinids are symbiotic polychete annelids having hemoglobins as essential oxygen- and sulfide-carriers for their endosymbiotic bacteria. We analyzed the structure of the hemoglobins from two species of siboglinids: the monilifera Sclerolinum contortum and the frenulata Oligobrachia webbi (i.e. haakonmosbiensis) from Norwegian cold seeps. Measured by Multi-Angle Laser Light Scattering (MALLS)...

2017
Ekaterina Minaeva Zhanneta Zalutskaya Valentina Filina Elena Ermilova

Truncated hemoglobins constitute a large family, present in bacteria, in archaea and in eukaryotes. However, a majority of physiological functions of these proteins remains to be elucidated. Identification and characterization of a novel role of truncated hemoglobins in the model alga provides a framework for a more complete understanding of their biological functions. Here, we use quantitative...

2005

T HE NATURE of the transition from hemoglobin F synthesis to hemoglobin A synthesis in the fetus and newborn remains unknown. Although it is evident from the elution method developed by Kleihauer, Braun and Betke13 that hemoglobin F and hemoglobin A may coexist in single erythrocytes,24 quantitative data regarding the amounts of these hemoglobins in individual cells are lacking. An attempt to q...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1994
S L McCune M P Reilly M J Chomo T Asakura T M Townes

Two human hemoglobins designed to inhibit the polymerization of sickle hemoglobin (Hb S; alpha 2 beta S2) have been produced. Mutations that disrupt the ability of Hb S to form polymers were introduced into the normal human beta-globin gene by site-specific mutagenesis. These mutations affect the axial and lateral contacts in the sickle fiber. The recombinant hemoglobin designated anti-sickling...

2014
Nejat Akar

Two previous reviews by Altay and Akar concerning the " Abnormal Hemoglobins in Turkey " appeared in the journal several years ago [1,2]. Since then, several other variants have been reported in both international and national journals. The aim of this mini-review was to compile the newly published abnormal hemoglobins in the Turkish population since these two previous papers [1,2]. During the ...

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