Bauer F, Hofmann K
Bundesanstalt für Fleischforschung, Institut für Chemie und Physik, Kulmbach, Federal Republic of Germany.
Z Lebensm Unters Forsch. 1990 May;190(5):414-9. doi: 10.1007/BF01202559.
The heat stability of beef myoglobin was investigated by means of its solubility and intensity of protein bands separated by isoelectric focusing. A method for the sensitive determination of myoglobin in the extracts was developed based on its ability to form a red dye by the oxidative coupling of 2,4-dichlorophenol and 4-aminoantipyrine in the presence of hydrogen peroxide. By this method, myoglobin could be determined to a concentration of 0.01 mg/ml. For the detection of electro-focused myoglobins, o-dianisidine has proved to be the most sensitive compound. The myoglobin content of the extracts, according to the intensity of the myoglobin bands in the electrophoretic gel, decreased with increasing temperature and heating-time. However, the position of the bands was not changed by the heat treatment.
通过肌红蛋白的溶解度和等电聚焦分离的蛋白质条带强度研究了牛肉肌红蛋白的热稳定性。基于肌红蛋白在过氧化氢存在下通过2,4 -二氯苯酚和4 -氨基安替比林的氧化偶联形成红色染料的能力，开发了一种灵敏测定提取物中肌红蛋白的方法。通过该方法，可测定浓度低至0.01 mg/ml的肌红蛋白。对于电聚焦肌红蛋白的检测，邻联茴香胺已被证明是最灵敏的化合物。根据电泳凝胶中肌红蛋白条带的强度，提取物中的肌红蛋白含量随温度升高和加热时间的增加而降低。然而，热处理并未改变条带的位置。
