Introduction：Basic information about HEMOGLOBIN CAS 9008-02-0, including its chemical name, molecular formula, synonyms, physicochemical properties, and safety information, etc.
HEMOGLOBIN Basic information
| Product Name: | HEMOGLOBIN |
| Synonyms: | Hemoglobin from porcine blood;Hemoglobin from turkey;Hemoglobin from rat,Hb;Hemoglobin porcine,Hb;Hemoglobin human,Hb;Hemoglobin (Bovine, 2*cryst);HEMOGLOBIN FROM BOVINE BLOOD, PGE. WITH 100 G*;HEMOGLOBIN DOG |
| CAS: | 9008-02-0 |
| MF: | C13H10N2O2 |
| MW: | 226.2307 |
| EINECS: | 293-254-9 |
| Product Categories: | Nitric Oxide Scavengers;Nitric Oxide ScavengersCell Signaling Enzymes;Nitric Oxide and Cell Stress;Nitric Oxide Metabolism |
| Mol File: | 9008-02-0.mol |
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HEMOGLOBIN Chemical Properties
| storage temp. | 2-8°C |
| solubility | 0.6 M HCl: soluble20mg/mL |
| form | substrate powder |
| color | Dark brown powder |
| biological source | Porcine |
| Water Solubility | Soluble in water. |
| Cosmetics Ingredients Functions | SKIN CONDITIONING |
| InChI | InChI=1S/C13H10N2O2/c1-8-4-5-9-11(16)7-10(15-13(9)14-8)12-3-2-6-17-12/h2-7H,1H3,(H,14,15,16) |
| InChIKey | INGWEZCOABYORO-UHFFFAOYSA-N |
| SMILES | N1C2=C(C=CC(C)=N2)C(=O)C=C1C1=CC=CO1 |
| EPA Substance Registry System | Hemoglobins (9008-02-0) |
Safety Information
| Hazard Codes | B |
| Safety Statements | 22-24/25 |
| WGK Germany | 3 |
| F | 1-10 |
| TSCA | TSCA listed |
| HS Code | 3002905150 |
| Storage Class | 11 - Combustible Solids |
HEMOGLOBIN Usage And Synthesis
| Description | Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chainscontains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operateindependently. The release (and binding) of oxygen is a cooperative process, which means that the loss(uptake) of the first oxygen molecule triggers the release of the remaining three.
The current model for oxygen binding in haemoglobin and myoglobin can be explained in the followingway. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane withits four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue.Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe3+ centre and O2 isreduced to [O2]-. Both species contain an unpaired electron. The low-spin Fe3+ moves into the plane andpulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygenin the other three haeme groups. |
| Uses | 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. It is used as a coloring agent for pet foods, a natural source of iron for nutraceuticals, a protein source for non-ruminant animals, and as a raw material for pharmaceutical porphyrin derivative production. |
| Uses | Medicine, usually called hemoglobin. |
| Uses | 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
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| Definition | The respiratory protein of the red blood cells, it transfers oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its affinity for carbon monoxide is >200 times that for oxygen. Hemoglobin is a conjugated protein of molec |
| Definition | The pigment of the redblood cells that is responsible for the transportof oxygen from the lungs to the tissues.It consists of a basic protein, globin,linked with four heme groups. Heme is acomplex compound containing an ironatom.The most important property of hemoglobinis its ability to combine reversiblywith one molecule of oxygen per iron atomto form oxyhemoglobin, which has abright red color. The iron is present in thedivalent state (iron(II)) and this remainsunchanged with the binding of oxygen.There are variations in the polypeptidechains, giving rise to different types of hemoglobinsin different species. The bindingof oxygen depends on the oxygen partialpressure; high pressure favors formation ofoxyhemoglobin and low pressure favorsrelease of oxygen. |
| Definition | One of a group ofglobular proteins occurring widely inanimals as oxygen carriers in blood.Vertebrate haemoglobin comprisestwo pairs of polypeptide chains,known as α-chains and β-chains(forming the globin protein), witheach chain folded to provide a bindingsite for a haem group. Each ofthe four haem groups binds oneoxygen molecule to form oxyhaemoglobin.Dissociation occurs inoxygen-depleted tissues: oxygen is releasedand haemoglobin is reformed.The haem groups also bind other inorganicmolecules, including carbonmonoxide (to form carboxyhaemoglobin).In vertebrates, haemoglobinis contained in the red blood cells(erythrocytes). |
| General Description | Native hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. |
| Biochem/physiol Actions | 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. |
| Purification Methods | Purify it from blood using CM-32 cellulose column chromatography. [Matsukawa et al. J Am Chem Soc 107 1108 1985.] For the purification of the and chains see Hill et al. Biochemical Preparations 10 55 1963. Histones (from S4A mouse lymphoma). The purification of histones uses a macroprocess column, heptafluorobutyric acid as solubilising and ion-pairing agent and an acetonitrile gradient. [McCroskey et al. Anal Biochem 163 427 1987.] |
HEMOGLOBIN Preparation Products And Raw materials
| Preparation Products | L-Leucine-->Chorionic Gonadotropin-->L-Histidine hydrochloride monohydrate-->Superoxide dismutase-->Hematoprophyrin-->hemoglobin, Vitreoscilla-->L-Histidine hydrochloride |
