Hemoglobins
Hemoglobins
CAS: 9008-02-0
Molecular Formula: C13H10N2O2
Hemoglobins - Names and Identifiers
Hemoglobins - Physico-chemical Properties
| Molecular Formula | C13H10N2O2 |
| Molar Mass | 226.2307 |
| Water Solubility | Soluble in water. |
| Solubility | 0.6 M HCl: soluble20mg/mL |
| Appearance | substrate powder |
| Color | Dark brown powder |
| Storage Condition | 2-8°C |
| MDL | MFCD00131282 |
Hemoglobins - Risk and Safety
| Safety Description | S22 - Do not breathe dust. S24/25 - Avoid contact with skin and eyes. |
| WGK Germany | 3 |
| FLUKA BRAND F CODES | 1-10 |
| TSCA | Yes |
| HS Code | 3002905150 |
Hemoglobins - Reference Information
| introduction | hemoglobin (Hb) is an oxygen-carrying protein mainly found in red blood cells of vertebrates and has the function of transporting oxygen and CO2. Yeast, paramecium, and many invertebrates also have hemoglobin. In 1945, Chinese scientist Wang Yinglai and British scientist D. Keeling isolated legume hemoglobin from root nodules of legumes. Hemoglobin is a pigment protein contained in human red blood cells. The most commonly used method for measuring hemoglobin is colorimetry. Through a blood cell analyzer, the concentration of hemoglobin can be automatically analyzed. Clinically, hemoglobin is an indicator of whether a person is anemic. The concentration of hemoglobin in normal adult men is 120-160g/L, and that in adult women is 110-150g/L. If it is lower than the normal range, hemoglobin is reduced, that is, anemia. |
| Molecular structure | Hemoglobin is a binding protein composed of heme and globin. There are two kinds of globin peptide chain, one is α chain, which is composed of 141 amino acids; the other is non-α chain (β chain, γ chain and δ chain), each with 146 amino acids. Various peptide chains have a fixed amino acid sequence, and the globin peptide chain composition of different hemoglobin is different. Each peptide chain is connected to a heme to form a hemoglobin subunit. Human hemoglobin is a tetramer composed of 4 subunits. |
| Function | Hemoglobin, as a blood substitute, has osmotic activity and the ability to transport and transfer oxygen, but it has the circulation through the renal route and through the blood vessel wall The shortcomings of rapid elimination result in a very short, therefore, typically unsatisfactory half-life. Further, human hemoglobin is also often contaminated with toxic levels of endotoxin, bacteria or viruses. Natural hemoglobin usually plays the role of carrying oxygen and releasing oxygen in red blood cells to supply the body's oxygen needs. Hemoglobin has a molecular weight of 64.5KD and contains four subunits, two α subunits and two β subunits. Each subunit in Hb is composed of a peptide chain and a heme molecule, and each heme molecule has a divalent iron. Hemoglobin containing divalent iron is called ferrous hemoglobin, which has the effect of carrying oxygen and releasing oxygen; the ferrous hemoglobin that binds oxygen is called oxyhemoglobin (O2Hb), and the ferrous hemoglobin that does not bind oxygen is called deoxyhemoglobin (HHb). Ferrous hemoglobin is easily converted into other forms of hemoglobin, such as methemoglobin (metHb)(hemoglobin in which divalent iron is oxidized to trivalent iron), and CO is combined to form carboxyhemoglobin (COHb), Combine with sulfide to form hemoglobin sulfide (SHb) and so on. What type of hemoglobin is not emphasized, usually refers to oxyhemoglobin. The main purpose of hemoglobin oxygen carrier is to overcome the nephrotoxicity of hemoglobin itself and replace the function of red blood cells carrying oxygen and releasing oxygen. At present, it is mainly used in the emergency treatment of patients with acute blood loss or instead of red blood cells when red blood cells are not available. The dosage is large and requires intravenous administration. |
| clinical significance | (1) physiological increase: newborn, plateau residence, etc. (2) Pathological increase: polycythemia vera, compensatory polycythemia. (3) Reduce: all kinds of anemia, leukemia, postpartum, after blood loss, etc. |
| use | properties: reddish brown powder is an iron-containing compound allosteric protein of vertebrate red blood cells, which is formed by combining heme and globin. globin accounts for about 96% and heme for 4%. Contains four polypeptide chains, each polypeptide chain contains a heme group, and iron in heme is divalent. When combined with oxygen, its chemical valence remains unchanged, forming oxyhemoglobin. It is bright red and has a light blue color after dissociation from oxygen. Use: biochemical research. Can break cell walls. |
| EPA chemical information | Information provided by: ofmpub.epa.gov (external link) |
Last Update：2024-04-10 22:29:15
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Featured ProductsMultiple SpecificationsSpot supply
Product Name: Hb Visit Supplier Webpage Request for quotationCAS: 9008-02-0
Tel: 18301782025
Email: 3008007409@qq.com
Mobile: 18021002903
QQ: 3008007409
Wechat: 18301782025
Spot supply
Product Name: Hemoglobin Protease Substrate Visit Supplier Webpage Request for quotationCAS: 9008-02-0
Tel: 0714-3999186
Email: 2853786052@qq.com
Mobile: 86+15671228036
QQ: 2853786052
Wechat: 15671228036
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