Thermal denaturation of alpha-crystallin.
Copyright policy )Thermal denaturation of alpha-crystallin.
Low 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. Viscosimetric study and ultraviolet absorption spectroscopy also indicated irreversible denaturation.
- Adelphi University United States
Protein Denaturation, Hot Temperature, Calorimetry, Differential Scanning, Light, Viscosity, Animals, Scattering, Radiation, Cattle, Spectrophotometry, Ultraviolet, Crystallins
Protein Denaturation, Hot Temperature, Calorimetry, Differential Scanning, Light, Viscosity, Animals, Scattering, Radiation, Cattle, Spectrophotometry, Ultraviolet, Crystallins
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).0 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!