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About This Item
Form:
substrate powder
Biological source:
bovine blood
Mol wt:
Mr ~64500
biological source
bovine blood
Quality Level
form
substrate powder
mol wt
Mr ~64500
technique(s)
activity assay: suitable
solubility
H2O: soluble 20 mg/mL
suitability
suitable for protease substrate
storage temp.
2-8°C
Gene Information
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 every 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 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.
Biochem/physiol Actions
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, 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.
Preparation Note
Prepared from washed, lysed and dialyzed erythrocytes.
Disclaimer
Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
监管及禁止进口产品
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Protocols
本方法可用于以血红蛋白为底物的胃蛋白酶活性测定。这是一种分光光度速率终止测定法。
This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.
Proteinase K activity measured via spectrophotometry using hemoglobin substrate, crucial for enzyme characterization.
Related Content
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)
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)
Global Trade Item Number
| SKU | GTIN |
|---|---|
| H2625-100G | 04061838820259 |
| H2625-1KG | 04061826718384 |
| H2625-25G | 04061835516070 |