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Key Documents

51290

Sigma-Aldrich

Hemoglobin from bovine blood

lyophilized, 2×cryst., ≥90% (SDS-PAGE), powder

Synonyme(s) :

Bovine hemoglobin, Hb, Methemoglobin

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About This Item

Numéro CAS:
9008-02-0
Numéro MDL:
MFCD00131282
Code UNSPSC :
12352202

Source biologique

bovine blood

Niveau de qualité

100

Pureté

≥90% (SDS-PAGE)

Forme

powder

Qualité

2×cryst.
lyophilized

Poids mol.

Mr ~64500

Technique(s)

UV/Vis spectroscopy: suitable

Impuretés

salt, none detected
~0.3% Fe

Perte

≤8% loss on drying

Numéro d'accès UniProt

P01966
P02070
P02081
P06642
P06643

Température de stockage

2-8°C

Informations sur le gène

cow ... HBA1(281221) , HBB(280813) , HBE2(513240) , HBE4(513108) , HBG(511735) , alpha globin(512439)

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Description générale

Hemoglobin (Hb) is the protein responsible for storage and transport of oxygen and other gaseous ligands in red blood cells (RBC). Hb is also the pioneer material for synthesis of Hb-based oxygen carriers (HBOCs) that can be used as substitutes for RBC.

Application

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

Actions biochimiques/physiologiques

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.

Autres remarques

Review: Oxygen carrier proteins
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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

Paul W Buehler et al.
Biomaterials, 31(13), 3723-3735 (2010-02-13)
Hemoglobin-based oxygen carriers (HBOC) are currently being developed as red blood cell (RBC) substitutes for use in transfusion medicine. Despite significant commercial development, late stage clinical results of polymerized hemoglobin (PolyHb) solutions hamper development. We synthesized two types of PolyHbs
M. Brunori et al.
Topics in Molecular and Structural Biology, 7, 263-263 (1985)
Toru Yamada et al.
PloS one, 7(11), e50271-e50271 (2012-11-28)
In conventional functional near-infrared spectroscopy (fNIRS), systemic physiological fluctuations evoked by a body's motion and psychophysiological changes often contaminate fNIRS signals. We propose a novel method for separating functional and systemic signals based on their hemodynamic differences. Considering their physiological
Xiao-Su Hu et al.
Journal of biomedical optics, 18(1), 17003-17003 (2013-01-08)
The reduction of trial-to-trial variability (TTV) in task-evoked functional near-infrared spectroscopy signals by considering the correlated low-frequency spontaneous fluctuations that account for the resting-state functional connectivity in the brain is investigated. A resting-state session followed by a task-state session of
Konstantinos Balaskas et al.
The British journal of ophthalmology, 97(5), 558-560 (2012-11-10)
This study examines the differences in spectral absorption properties between the maculae of patients with active neovascular macular degeneration and those with early age related maculopathy (ARM). Patients attending for management of neovascular age related macular degeneration (AMD) underwent multispectral
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Chromatograms

application for HPLC

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