Literature DB >> 11233563

Gamma radiation effects on alpha-lactalbumin: structural modifications.

A Chapelier1, M Desmadril, C Houée-Levin.   

Abstract

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.

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Year:  2001        PMID: 11233563

Source DB:  PubMed          Journal:  Can J Physiol Pharmacol        ISSN: 0008-4212            Impact factor:   2.273


  2 in total

1.  Chemical analysis of solid-state irradiated human insulin.

Authors:  Hélène Terryn; Jean-Paul Vanhelleputte; Aubert Maquille; Bernard Tilquin
Journal:  Pharm Res       Date:  2006-08-09       Impact factor: 4.200

Review 2.  Age-related cataracts: Role of unfolded protein response, Ca2+ mobilization, epigenetic DNA modifications, and loss of Nrf2/Keap1 dependent cytoprotection.

Authors:  Palsamy Periyasamy; Toshimichi Shinohara
Journal:  Prog Retin Eye Res       Date:  2017-08-31       Impact factor: 21.198

  2 in total

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