Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells

In English

Författare

Summary, in English

This study characterized a protein complex in human milk that induces apoptosis in tumor cells but spares healthy cells. The active fraction was purified from casein by anion exchange chromatography. Unlike other casein components the active fraction was retained by the ion exchanger and eluted after a high salt gradient. The active fraction showed N-terminal amino acid sequence identity with human milk alpha-lactalbumin and mass spectrometry ruled out post-translational modifications. Size exclusion chromatography resolved monomers and oligomers of alpha-lactalbumin that were characterized using UV absorbance, fluorescence, and circular dichroism spectroscopy. The high molecular weight oligomers were kinetically stable against dissociation into monomers and were found to have an essentially retained secondary structure but a less well organized tertiary structure. Comparison with native monomeric and molten globule alpha-lactalbumin showed that the active fraction contains oligomers of alpha-lactalbumin that have undergone a conformational switch toward a molten globule-like state. Oligomerization appears to conserve alpha-lactalbumin in a state with molten globule-like properties at physiological conditions. The results suggest differences in biological properties between folding variants of alpha-lactalbumin.

Publiceringsår

1999-03-05

Språk

Engelska

Sidor

96-6388

Publikation/Tidskrift/Serie

Journal of Biological Chemistry

Volym

274

Issue

10

Dokumenttyp

Artikel i tidskrift

Förlag

American Society for Biochemistry and Molecular Biology

Ämne

  • Biochemistry and Molecular Biology

Nyckelord

  • Amino Acid Sequence
  • Apoptosis
  • Dimerization
  • Female
  • Humans
  • Lactalbumin
  • Milk, Human
  • Molecular Sequence Data
  • Neoplasms
  • Protein Folding
  • Structure-Activity Relationship

Status

Published

Forskningsgrupp

  • Experimental Infection Medicine, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 0021-9258