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H4632

Sigma-Aldrich

Hemoglobin equine

lyophilized powder

Synonyme(s) :

Hb

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

horse

Forme

lyophilized powder

Technique(s)

protein quantification: suitable

Solubilité

H2O: soluble 10 mg/mL

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

Description générale

Hemoglobin is the major component of red blood cells and is responsible for their red color. Its normal concentration in erythrocytes is 34%. The structure of horse hemoglobin was elucidated first. It comprises heme (iron protoporphyrin IX group) and four polypeptide chains. The fetal and adult hemoglobin of horse are structurally identical.

Application

Hemoglobin equine has been used as a standard protein:
  • to test solid-film sampling methodology in Fourier transform infrared spectroscopy (FT-IR) for protein secondary structure determination
  • in capillary reversed-phase liquid chromatography-tandem mass spectrometry (LC/MS/MS) post enzymatic digestion
  • for quantification of hemoglobin content from the planktonic crustacean, Daphnia magna

Actions biochimiques/physiologiques

Hemoglobin is the most important respiratory protein of vertebrates by its ability to transport oxygen from the lungs to body tissues and to facilitate the return transport of carbon dioxide. The ferrous-ferric (Fe2+/Fe3+) balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to nitric oxide (NO), a vasodilator which enhances blood flow to oxygen-deprived tissues. The fetal and adult hemoglobin from horse display differences in their affinity towards 2,3-diphosphoglycerate (2,3-DPG). Mutation in the globin gene is implicated in sickle cell anemia.
Oxygen transporter, NO scavenger

Attention

Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Yan Zhang et al.
Zoological science, 20(9), 1087-1093 (2003-10-28)
The physiological significance of the position and shape of the oxygen equilibrium curve (OEC) of horse hemoglobin (Hb) is considered from the viewpoint of oxygen (O2) transport efficiency and the effectiveness of the Bohr effect. In horse fetal and maternal
Alain J Marengo-Rowe
Proceedings (Baylor University. Medical Center), 19(3), 239-245 (2007-01-26)
In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of
Brita T A Muyssen et al.
Ecotoxicology and environmental safety, 73(5), 735-742 (2010-01-12)
Effects of temperature and Cd acclimation (>or=6 generations) on life history and tolerance responses to stress in three clones of Daphnia magna was examined using a 2x2 design (20 and 24 degrees C, 0 and 5 microg L(-1) Cd). Endpoints
Alan N Schechter
Blood, 112(10), 3927-3938 (2008-11-08)
Much of our understanding of human physiology, and of many aspects of pathology, has its antecedents in laboratory and clinical studies of hemoglobin. Over the last century, knowledge of the genetics, functions, and diseases of the hemoglobin proteins has been
Pavel V Bondarenko et al.
Analytical chemistry, 74(18), 4741-4749 (2002-09-28)
In this report, we describe an approach for identification and relative quantitation of individual proteins within mixtures using LC/MS/MS analysis of protein digests. First, the proteins are automatically identified by correlating the tandem mass spectra with peptide sequences from a

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