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Key Documents

H2625

Sigma-Aldrich

Hemoglobin from bovine blood

suitable for protease substrate, substrate 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

substrate powder

Poids mol.

Mr ~64500

Technique(s)

activity assay: suitable

Solubilité

H2O: soluble 20 mg/mL

Adéquation

suitable for protease substrate

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 every 141 and 146 amino acids respectively. It exists as a tetramer with each monomer having heterocyclic porphyrin ring with iron constituting the heme.
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 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.

Application

Hemoglobin from bovine blood has been used as a substrate in cathepsin D activity assay. It has also been used to measure the activity of acid proteases (pepsin-like) in the stomach extract.
The solubility of α-elastin has been applied to construction of elastin-mimetic biomaterials.

Actions biochimiques/physiologiques

Bovine hemoglobin is used in the production of hemoglobin-vesicles (HbV). It has high thermal stability and high oxygen affinity when compared to human hemoglobin. Bovine hemoglobin interacts with synthetic and azo dyes. Polymerized forms of bovine hemoglobin are used to treat 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.

Notes préparatoires

Prepared from washed, lysed and dialyzed erythrocytes.

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

P John Wright et al.
Journal of the American Society for Mass Spectrometry, 20(3), 484-495 (2008-12-23)
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been studied with H/D exchange and cross section measurements. During the H/D exchange measurements, tetramers undergo slow dissociation to dimers, and dimers to monomers, but this
Circadian cycle of digestive enzyme production at fasting and feeding conditions in Nile tilapia, Oreochromis niloticus (Actinopterygii: Perciformes: Cichlidae)
MEJIA, MAGNOLIA MONTOYA and others
Acta ichthyologica et piscatoria, 32(2), 188-193 (2016)
High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle
Fidalgo L, et al.
Czech Journal of Food Sciences, 32(2), 188-193 (2016)
Characteristics of bovine hemoglobin as a potential source of hemoglobin-vesicles for an artificial oxygen carrier
Sakai H, et al.
Journal of Biochemistry, 131(4), 611-617 (2002)
Xianbo Lu et al.
Biosensors & bioelectronics, 23(8), 1236-1243 (2007-12-18)
Carbon nanofibers (CNFs), with typical diameters of approximately 80 nm and lengths of the order of micrometers, are extremely attractive in bioanalytical area as they can combine properties of high surface area, non-toxicity, acceptable biocompatibility, ease of fabrication, chemical and

Articles

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Protocoles

Our General Protease Assay Procedures and Substrates overview.

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Chromatograms

application for HPLC

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