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Merck

H2500

Hemoglobin from bovine blood

lyophilized powder

Synonyme(s) :

Bovine hemoglobin, Hb, Methemoglobin

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352202
eCl@ss:
42030116
NACRES:
NA.61
MDL number:
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Nom du produit

Hemoglobin from bovine blood, lyophilized powder

biological source

bovine blood

form

lyophilized powder

mol wt

Mr ~64500

technique(s)

MALDI-TOF: suitable

UniProt accession no.

storage temp.

2-8°C

Quality Level

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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.

Biochem/physiol Actions

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, NO scavenger
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.

Disclaimer

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

General description

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.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Endogenous Interleukin-10 Deficiency Exacerbates Vascular Pathology in Traumatic Cervical Spinal Cord Injury
Badner A, et al.
Journal of Neurotrauma (2019)
Hao Zhang et al.
Science advances, 5(3), eaaw0873-eaaw0873 (2019-03-16)
Monitoring regional tissue oxygenation in animal models and potentially in human subjects can yield insights into the underlying mechanisms of local O2-mediated physiological processes and provide diagnostic and therapeutic guidance for relevant disease states. Existing technologies for tissue oxygenation assessments
Automating the application of smart materials for protein crystallization
Khurshid S, et al.
Acta Crystallographica Section D, Biological Crystallography, 71(3), 534-540 (2015)
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)

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