نتایج جستجو برای: hemoglobins

تعداد نتایج: 1615  

Journal: :Analytical biochemistry 1982
A Amanullah S Hanash K Bunnell J Strahler D L Rucknagel S J Ferruci

Ion-exchange high-performance liquid chromatography was employed as a screening method for abnormal hemoglobins in the newborn period. Samples of cord blood collected in EDTA tubes were used for this analysis. Hemolysates were injected onto 4.1 X loo-mm Synchropak ion-exchange columns using an automatic injector. Hemoglobin separation was carried out by means of a sodium acetate gradient. A tot...

Journal: :Clinical chemistry 1984
F A Garver H Singh H Moscoso D P Kestler B S McGuire

The presence and quantity of hemoglobins Barts and A2 in hemolysates from normal donors and individuals with alpha- and beta-thalassemia trait, respectively, were determined with an enzyme-labeled immunosorbent assay (ELISA). This technique requires the incorporation of monospecific antisera capable of specifically reacting only with these hemoglobins, e.g., with the delta chain of Hb A2 and ga...

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: :Genetics and molecular research : GMR 2010
P J A Zamaro C R Bonini-Domingos

We looked for abnormal hemoglobins in blood samples sent for diagnosis of anemia. Identification of the hemoglobins was made using electrophoretic, chromatographic and molecular procedures. The 2020 blood samples were of patients from various regions of Brazil and from some other Latin American countries. Among the abnormal hemoglobins that we found, 3.5% are known to be rare, while 51% had an ...

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: :The New phytologist 2011
Pilar Bustos-Sanmamed Alejandro Tovar-Méndez Martin Crespi Shusei Sato Satoshi Tabata Manuel Becana

• In legumes, symbiotic leghemoglobins facilitate oxygen diffusion to the bacteroids, but the roles of nonsymbiotic and truncated hemoglobins are largely unknown. Here the five hemoglobin genes of Lotus japonicus have been functionally characterized to gain insight into their regulatory mechanisms. • Plants were exposed to nitric oxide donors, stressful conditions, and hormones. Gene expression...

Journal: :The American journal of physiology 1974
H D Kim J Duhm

KIM, HYUN DJU, AND JOCHEN DUHM. Postnutal decrease in the oxygen a#nity of pig blood induced by red cell 2,3-DPG. Am. J. Physiol. 226(4): 1001-1006. 1974.-Blood and purified hemoglobins obtained from neonatal pigs, l-50 days old, and adult pigs have been examined in terms of intracellular organic phosphate, oxidation rate, Bohr coefficient, and oxygen affinity. It was found that the marked post...

Journal: :The Journal of General Physiology 1951
George Wald Austen Riggs

The blood hemoglobin of the sea lamprey presents a curious mixture of primitive and highly specialized properties. Like muscle hemoglobin, it has a molecular weight of about 17,000, and apparently contains a single heme. Its isoelectric point is like that of a typical invertebrate hemoglobin. Its amino acid composition is partly characteristic of invertebrate) partly of vertebrate hemoglobins (...

Journal: :The Journal of biological chemistry 1994
M S Hargrove E W Singleton M L Quillin L A Ortiz G N Phillips J S Olson A J Mathews

To develop an assay for hemin dissociation, His64(E7) was replaced by Tyr in sperm whale myoglobin producing a holoprotein with a distinct green color due to an intense absorption band at 600 nm. Val68(E11) was replaced by Phe in the same protein to increase its stability. When excess Tyr64-Val68 apoglobin is mixed with either metmyoglobin or methemoglobin, the solution turns from brown to gree...

Journal: :molecular biology research communications 2014
mohammad reza dayer mohammad saaid dayer ali akbar moosavi-movahedi

hemoglobin is a porphyrin containing protein with an a2b2 tetrameric structure and like other porphyrin compounds shows spectral behavior of species specific characteristics. researchers tend to relate bands in the hemoglobin spectra to certain structural and/or functional features. given the fact that hemoglobin is the main oxygen carrier in animals functioning through the oxy«deoxy equilibriu...

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