Gamma radiation effects on alpha-lactalbumin: structural modifications.
Alpha-lactalbumin was irradiated in the lyophilized state in air at ambient temperature. The irradiated protein was examined by size exclusion chromatography, sodium dodecyl sulfate polyacrylamide gel electrophoresis, circular dichroism, and microcalorimetry. Irradiation induced the loss of aromatic amino acids and of helicity so that fragmentation and aggregation products were obtained. The thermodynamic properties of the protein were also modified. The irradiated protein had lower stability, however, the temperature at which denaturation occurred process remained constant.
Chapelier
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Laboratoire de Chimie Physique, UMR 8611, CNRS-Université Paris-Sud, Orsay, France.
Desmadril
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Houée-Levin
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D002151:Calorimetry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005720:Gamma Rays; D006863:Hydrogen-Ion Concentration; D007768:Lactalbumin / Q000737:chemistry* / Q000528:radiation effects*; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet; D014508:Urea / Q000737:chemistry
D014508:Urea; D007768:Lactalbumin