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Thermal denaturation of alpha-crystallin.
Lens and eye toxicity research, 1991Low molecular weight alpha-crystallin, isolated from cow lenses, exhibit irreversible thermal denaturation in solution at 75 degrees C. The heat of denaturation was obtained from a differential scanning calorimetric endothermic peak. A second run on the denatured alpha-crystallin solution showed that the denaturation is irreversible.
J A, Castoro, F A, Bettelheim
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Effects of Thermal Denaturation on Binding between Bixin and Whey Protein
Journal of Agricultural and Food Chemistry, 2012Yue Zhang, Qixin Zhong
exaly
Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05
BBA - Proteins and Proteomics, 1995Carl Holt, Peter Sellers
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Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin
Biophysical Chemistry, 1989Savo Lapanje +2 more
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Thermal denaturation of bovine immunoglobulin G and its association with other whey proteins
Food Hydrocolloids, 2017Dimuthu Bogahawaththa +2 more
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Thermal denaturation of deionized and native purple membranes
Biochimica Et Biophysica Acta - Biomembranes, 1988Josep Cladera, Esteve Padrós
exaly
Thermal denaturation of fish collagen in solution: A calorimetric and kinetic analysis
Thermochimica Acta, 2014Wentao Liu, Zhenhua Tian, Conghu Li
exaly
Monitoring protein denaturation using thermal conductivity probe
International Journal of Biological Macromolecules, 2013Namwoo Yi, Jaesung Park, Dongsik Kim
exaly