Myoglobin
Myoglobin
CAS: 100684-32-0
Molecular Formula:
Myoglobin - Names and Identifiers
Myoglobin - Physico-chemical Properties
| Water Solubility | Soluble in water |
| Solubility | H2O: 10 mg/mL, clear, red to red-brown |
| Appearance | essentially salt-free, lyophilized powder |
| Storage Condition | -20°C |
| MDL | MFCD00131643 |
| Use | Overview Myoglobin is a protein that stores oxygen in mammalian muscles. It is especially abundant in diving mammalian muscles, causing the muscles to be brown. Myoglobin is composed of a polypeptide chain and a heme auxiliary group, with a molecular weight of 16700 and 153 amino acid residues. The subunits of myoglobin and hemoglobin have obvious homology in amino acid sequence, and their conformation and function are also very similar. The molecular configuration of myoglobin is dense and strong, and the amino acid residues containing the side chains of hydrophilic groups are almost all on the outer surface of the molecule, which just binds to water molecules to make it a soluble protein. |
Myoglobin - 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 |
Myoglobin - Reference
| Reference Show more | 1. Liu Xie, Guo Yunlong, Xu Qingxuan, etc. Study on the analytical properties of melon seed shell as a new type of wood electrospray material [J]. Analytical Chemistry, 2019(9). 2. Xia Lu, Xiaoye Wen, Zhefeng Fan,A sensitive biosensor based on a ferrocene-marked adapter for the flux detection of platelet-derived growth factor BB,Journal of Luminal, Volume 221,2020,117042,ISSN 0022-2313,https://doi.org/10.1016/j.jlu 3. [IF = 3.205] Dandan Lan et al."Preparation of a hydroxyethyl-based monolithic column and its application in the isolation of intact proteins from complex bio-samples."J Chromatogr B. 2019 Jan;1104:89 4. [IF=3.28] Xia Lu et al."A sensitive biosensor based on a ferrocene-marked adapter for the fluorescence detection of platelet-derived growth factor BB."J Lumin. 2020 May;221:117042 |
Myoglobin - Uses and synthesis methods
structure
Myoglobin is a binding protein composed of a peptide chain and a heme auxiliary group. It is a protein that stores oxygen in the muscle. Its oxygen saturation curve is hyperbolic. Myoglobin is found in muscle and is particularly abundant in myocardium. The tertiary structure of sperm whale myoglobin was elucidated by Kendrew using X-ray diffraction in 1960. This is the world's first described protein tertiary junction. Because the tertiary structure is directly related to the biological function of protein, and the analysis of the tertiary structure is very difficult, this work has been highly evaluated by the academic community.
Physiological function
myoglobin is a monomer protein with a relative molecular weight of 17000. it mainly exists in the cytoplasm of skeletal muscle and myocardial cells, and a small amount exists in thyroid and thymus. the content in skeletal muscle is 3~9 mg/g, the content in thyroid gland is 0.04~0.11 mg/g, the content in thymus is 0.01~0.05 mg/g, the content in smooth muscle cells does not contain myoglobin, and the content in normal human serum is very small, because of its small molecular weight, it is mainly metabolized and excreted in the kidney, partly metabolized by the reticuloendothelial system, and its decomposition process is similar to hemoglobin. It forms the hemoglobin family together with globulin, globin and neuroglobin. These oxygen binding proteins are found in almost all vertebrates. Hemoglobin is localized within red blood cells, but it has recently been found to be present in a variant of arterial endothelial cells. It is worth noting that myoglobin is also found in non-muscle cells, such as fish brain cells, kidney, liver and human breast tumor cells. During the occurrence and development of mouse embryos, myoglobin is expressed in the ventricle, less in the atrium, and the expression in the ventricle is also gradient. In the heart of adult mice, there is a systematic expression in the atria and ventricles, and the expression in the endocardium and epicardium is not different. In contrast, myoglobin is expressed spatially in the human adult heart, and is expressed more in the endocardium than in the epicardium. This may suggest that higher myoglobin is required in the endocardium of the heart to regulate the oxygen supply to support the blood flow of the heart in time and space.
application
the diagnosis and prediction of myoglobin for early myocardial infarction and reinfarction; myoglobin stores and transports oxygen; myoglobin can control the dynamic balance of myocardial nitric oxide.
Last Update：2024-04-10 22:29:15
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