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H2500

Sigma-Aldrich

Hemoglobin from bovine blood

lyophilized powder

Synonyme(s) :

Bovine hemoglobin, Hb, Methemoglobin

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
eCl@ss :
42030116
Nomenclature NACRES :
NA.61

Source biologique

bovine blood

Niveau de qualité

Forme

lyophilized powder

Poids mol.

Mr ~64500

Technique(s)

MALDI-TOF: suitable

Numéro d'accès UniProt

Température de stockage

2-8°C

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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%. Hemoglobin is a globular protein with α and β chains with each 141 and 146 amino acids, respectively. It exists as a tetramer with each monomer having heterocyclic porphyrin ring with iron constituting the heme.

Application

Hemoglobin from bovine blood has been used in:
  • standard curve generation for the quantification intraparenchymal hemorrhage and parenchymal hemorrhage in spinal cord homogenate using Drabkin′s assay, Quadrupole-Ion Mobility-Time-of-Flight mass spectrometery
  • the generation of molecularly imprinted polymers (MIPs) to mimic high molecular-weight polyethylene glycol (PEG) in crystallization studies

The solubility of α-elastin has been applied to construction of elastin-mimetic biomaterials.

Actions biochimiques/physiologiques

Hemoglobin is the most important respiratory protein of vertebrates by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport of carbon dioxide. Bovine hemoglobin is used in the generation of hemoglobin-vesicles (HbV) for oxygen transport. It is thermally stable and displays high affinity to oxygen when compared to human hemoglobin. Bovine hemoglobin interacts with synthetic and azo dyes. Polymerized forms of bovine haemoglobin is recommended for treating autoimmune hemolytic anemia.
Oxygen transporter. The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation; deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues.

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)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Characteristics of bovine hemoglobin as a potential source of hemoglobin-vesicles for an artificial oxygen carrier
Sakai H, et al.
The Journal of biological chemistry, 131(4), 611-617 (2002)
Extensive charge reduction and dissociation of intact protein complexes following electron transfer on a quadrupole-ion mobility-time-of-flight MS
Lermyte F, et al.
Journal of the American Society For Mass Spectrometry, 26(7), 1068-1076 (2015)
A study of the interaction of bovine hemoglobin with synthetic dyes using spectroscopic techniques and molecular docking
Bansal S, et al.
Frontiers in Chemistry, 4, 50-50 (2017)
Arjen Amelink et al.
Journal of biomedical optics, 13(5), 054051-054051 (2008-11-22)
We have developed a new technique, fluorescence differential path length spectroscopy (FDPS), that enables the quantitative investigation of fluorophores in turbid media. FDPS measurements are made with the same probe geometry as differential path length spectroscopy (DPS) measurements. Phantom measurements
Early Intravenous Infusion of Mesenchymal Stromal Cells Exerts a Tissue Source Age-Dependent Beneficial Effect on Neurovascular Integrity and Neurobehavioral Recovery After Traumatic Cervical Spinal Cord Injury
Vawda R, et al.
Stem Cells Translational Medicine (2019)

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