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A Novel Sickle Hemoglobin: Hemoglobin S-South End

Journal of Pediatric Hematology/Oncology, 2004
Sickle hemoglobin (Hb S; beta Glu6Val) is due to an AGTG; beta Lys132Asn, AAA>AAC). When present alone, the beta Lys132Asn mutation has low oxygen affinity. Therefore, this mutation may enhance the polymerization of the Hb S variant. Furthermore, the variant hemoglobin mimics Hb A on high-pressure liquid chromatography, and its identity is not easily ...
Hong-Yuan, Luo   +7 more
openaire   +2 more sources

The Relationship of Hemoglobin A1C to Time-in-Range in Patients with Diabetes

Diabetes Technology & Therapeutics, 2019
Background: There has been recent recognition of the limitations of hemoglobin A1C (HbA1C) in describing both short- and long-term glycemic control. Continuous glucose monitoring (CGM) provides robust data about short-term glycemic control and provides ...
R. Vigersky, Chantal M. Mcmahon
semanticscholar   +1 more source

Hemoglobin Mahidol: a new hemoglobin α-chain mutant

Canadian Journal of Biochemistry, 1970
A slow (less anionic) hemoglobin mutant has been detected by starch gel electrophoresis of hemoglobin from three unrelated patients in Bangkok. Dissociation of the abnormal hemoglobin with p-hydroxymercuribenzoate showed that the α-chain was the site of the mutation.
S, Pootrakul, G H, Dixon
openaire   +2 more sources

Hemoglobin C-I-A

Acta Haematologica, 1980
Hemoglobin I (alpha 16 lys leads to glu) was identified in association with hemoglobins C and A in a black American woman who had no clinical or hematologic disease. Her erythrocytes contained four major hemoglobins, all of which were separable by DEAE-cellulose column chromatography.
G R, Honig, M, Borders
openaire   +2 more sources

Xenopus laevis hemoglobin and its hybrids with hemoglobin A

Biochemistry, 1987
Isolated 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
Condò SG   +3 more
openaire   +4 more sources

A study on serum hemoglobin and hemoglobin-binding capacity

Clinica Chimica Acta, 1964
Abstract Methods have been proposed to measure hemoglobin in serum in the range of 2–20 mg/100 ml. The effect of haptoglobin-binding on the peroxidase activity of hemoglobin and the need for proper calibration standards have been discussed. Serum hemoglobin and haptoglobin concentrations should be performed simultaneously.
A, LUPOVITCH, B, ZAK
openaire   +2 more sources

Hemoglobin Monza: A New Variant of Unstable Hemoglobin

Blood, 2023
Introduction: Unstable hemoglobins are variants with structural abnormalities; while not hindering protein formation, they lead to protein destabilization and can cause hemolytic crises. Most unstable hemoglobins are caused by point mutations that result in the premature dissociation of heme from the globin chain and ...
Ivan Civettini   +15 more
openaire   +1 more source

Priapism in a patient with unstable hemoglobin: Hemoglobin Köln

American Journal of Hematology, 2003
AbstractWe report a case of severe priapism occurring in a patient with unstable hemoglobin, hemoglobin Köln, and underline several factors that may have contributed to this complication: abnormal plasticity of red cells, splenectomy, and cytomegalovirus infection. Since emergency treatment may prevent impotence, patients and parents should be educated
Valérie, Andrieu   +2 more
openaire   +2 more sources

Fetal Hemoglobin Alters Hemoglobin A1c Measurements

Annals of Internal Medicine, 1991
Excerpt To the editors:The letter of Holt and colleagues (1) emphasizes that diabetic subjects with hemoglobin S or C traits will have a falsely low hemoglobin A1cvalue if measured by certain metho...
R W, Bergstrom, J R, Kelley, W K, Ward
openaire   +2 more sources

A PEGylated bovine hemoglobin as a potent hemoglobin‐based oxygen carrier

Biotechnology Progress, 2016
Hemoglobin (Hb)‐based oxygen carriers (HBOCs) have been used as blood substitutes in surgery medicine and oxygen therapeutics for ischemic stroke. As a potent HBOC, the PEGylated Hb has received much attention for its oxygen delivery and plasma expanding ability.
Ying, Wang   +10 more
openaire   +2 more sources

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