Differential scanning calorimetric studies on thermal behaviors of myofibrillar proteins.
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چکیده
منابع مشابه
Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation.
Thermal stability of Momordica charantia seed lectin (MCL) was investigated as a function of protein concentration, pH, scan rate, and at different ligand concentrations by using high-sensitivity differential scanning calorimetry (DSC). The DSC endotherm obtained at pH 7.4 consists of two entities with transition temperatures at ca. 333.7 K, and 338 K. The unfolding process is irreversible and ...
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ژورنال
عنوان ژورنال: NIPPON SUISAN GAKKAISHI
سال: 1985
ISSN: 1349-998X,0021-5392
DOI: 10.2331/suisan.51.1841