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Merck

H2625

Sigma-Aldrich

Hemoglobin from bovine blood

suitable for protease substrate, substrate powder

Synonim(y):

Bovine hemoglobin, Hb, Methemoglobin

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About This Item

Numer CAS:
Numer MDL:
Kod UNSPSC:
12352202
eCl@ss:
42030116
NACRES:
NA.61

pochodzenie biologiczne

bovine blood

Poziom jakości

Postać

substrate powder

masa cząsteczkowa

Mr ~64500

metody

activity assay: suitable

rozpuszczalność

H2O: soluble 20 mg/mL

przydatność

suitable for protease substrate

numer dostępu UniProt

temp. przechowywania

2-8°C

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Opis ogólny

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.

Zastosowanie

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.

Działania biochem./fizjol.

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.

Przestroga

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

Uwaga dotycząca przygotowania

Prepared from washed, lysed and dialyzed erythrocytes.
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

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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
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Characteristics of bovine hemoglobin as a potential source of hemoglobin-vesicles for an artificial oxygen carrier
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Produkty

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).

Protokoły

This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.

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).

Aktywność proteinazy K mierzona za pomocą spektrofotometrii przy użyciu substratu hemoglobiny, kluczowa dla charakterystyki enzymu.

Chromatograms

application for HPLC

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