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中文名(CN) 英文名(EN) CAS No. 规格(SP) 报价(CNY) 产地(From) 类别(Key)
肌红蛋白 Myoglobin from equine skeletal muscle (95-100%) 100684-32-0 100MG 466.00 Sigma-M0630 蛋白质
肌红蛋白 Myoglobin from equine skeletal muscle (95-100%) 100684-32-0 1G 1952.00 Sigma-M0630 蛋白质
肌红蛋白 Myoglobin from equine skeletal muscle (95-100%) 100684-32-0 5G 7580.00 Sigma-M0630 蛋白质

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中文名称 肌红蛋白
英文名称 Myoglobin from equine skeletal muscle (95-100%)
CAS识别号 100684-32-0
MDL识别号 MFCD00131643
EC识别号 309-705-0
Beilstein Null,without related properties.
分子式 Null,without related properties.
分子量 Null,without related properties.
分子结构图 分子图
产品性状 红棕色粉末,参考溶解度:10MG/ML.
质量标准 Myoglobin from horse skeletal muscle is a single chain heme protein containing 153 amino acid residues. It posesses no disulfide bridges or free -SH groups. Myoglobin contains 8 variously sized right-handed helical regions, joined by non-ordered or random coil regions. These 8 helices (A, B, C, D, E, F, G, H) are folded back on top of one another, and the heme is situated between helices E and F. The heme is almost totally buried. Only the edge carrying the two
hydrophylic propionic acid groups is exposed. The heme is held in position by a coordinating complex between the central Fe(II) atom and 2 histidine,residues (on helices E and F, respectively). One of these histidines binds to the oxygen of the water molecule, which is bound to the heme. The position and the functional competence of the heme depends on the hydrophobic amino acids that line the inside of the heme pocket. The function of myoglobin is oxygen storage and transfer (from hemoglobin to respiratory ezymes). The affinity of myoglobin for oxygen is higher than that of hemoglobin.4 Slight changes in the tertiary structure of myoglobin destroy the oxygen binding function of the heme. Metmyoglobin, myoglobin with Fe(III), does not bind oxygen. Myoglobin is found in skeletal muscle.4
储存条件 -20 °C 冷藏保存,Stored at -20 °C
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