Ultraviolet illumination-induced reduction of α-lactalbumin disulfide bridges

Prolonged exposure of Ca2+‐loaded or Ca2+‐depleted human α‐lactalbumin to ultraviolet light (270–290 nm, 1 mW/cm2, for 2 to 4 h) results in a 10‐nm red shift of its tryptophan fluorescence spectrum. Gel chromatography of the UV‐illuminated samples reveals two non‐native protein forms: (1) a componen...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2003-06, Vol.51 (4), p.498-503
Hauptverfasser:	Permyakov, Eugene A., Permyakov, Serge E., Deikus, Gintaras Y., Morozova-Roche, Ludmila A., Grishchenko, Valery M., Kalinichenko, Lina P., Uversky, Vladimir N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Calcium - metabolism cystein disulfide bridge Disulfides - chemistry Humans Lactalbumin - chemistry Lactalbumin - metabolism Mass Spectrometry - methods Oxidation-Reduction - radiation effects photo-induced modification Protein Binding - radiation effects Protein Conformation Temperature Thermodynamics tryptophan Ultraviolet Rays α-lactalbumin
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!