umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Ultraviolet illumination-induced reduction of alpha-lactalbumin disulfide bridges
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Show others and affiliations
2003 (English)In: Proteins: Structure, Function, and Bioinformatics, Vol. 51, no 4, 498-503 p.Article in journal (Refereed) Published
Abstract [en]

Prolonged exposure of Ca2+-loaded or Ca2+-depleted human -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 component with a red-shifted tryptophan fluorescence spectrum; and (2) a component with kynurenine-like fluorescent properties. The first component has from 0.6 to 0.9 free DTNB-reactive SH groups per protein molecule, which are absent in the native protein and is characterized by slightly lowered Ca2+-affinity (2 × 108 M-1 versus 8 × 108 M-1 for the native protein) and absence of observable thermal transition. The second component corresponds to the protein with photochemically modified tryptophan residues. It is assumed that the UV excitation of tryptophan residue(s) in -lactalbumin is followed by a transfer of electrons to the SS bonds, resulting in their reduction. Mass spectrometry data obtained for trypsin-fragmented UV-illuminated -lactalbumin with acrylodan-modified free thiol groups reveal the reduction of the 61-77 and 73-91 disulfide bridges. The effect observed has to be taken into account in any UV-region spectral studies of -lactalbumin. Proteins 2003;51:498-503.

Place, publisher, year, edition, pages
2003. Vol. 51, no 4, 498-503 p.
Keyword [en]
alpha-lactalbumin, tryptophan, cystein, disulfide bridge, photo-induced modification
Identifiers
URN: urn:nbn:se:umu:diva-9917DOI: doi:10.1002/prot.10371OAI: oai:DiVA.org:umu-9917DiVA: diva2:149588
Available from: 2008-05-22 Created: 2008-05-22 Last updated: 2011-03-30Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Authority records BETA

Morozova-Roche, Ludmila A

Search in DiVA

By author/editor
Morozova-Roche, Ludmila A
By organisation
Department of ChemistryDepartment of Medical Biochemistry and Biophysics

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 37 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf