Altered conformation of Gc (Vitamin D-binding protein) upon complexing with cellular actin

Pascal Goldschmidt-Clermont, Merfyn H. Williams, Robert M. Galbraith

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Complexing of serum Gc (Vitamin D-binding protein) with cellular actin can occur in the extracellular space as a result of cell turnover, and particularly cell necrosis. The clearance of such complexes is significantly more rapid than that of Gc alone, and several tissues are involved in their uptake, but the mechanisms involved are unknown. We present evidence here that interaction with actin results in alteration of certain physicochemical properties of Gc. Fluorescence of the hydrophobic probe 2-p-toluidinylnaphthylene-6-sulfonate was abolished by complex formation with actin. In addition, isoelectric focusing of complexes between Gc, and actin from different tissues, revealed that complexes were generally more acidic than either protein individually. These findings indicate that complexing of Gc with actin results in altered conformation.

Original languageEnglish
Pages (from-to)611-617
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume146
Issue number2
DOIs
StatePublished - Jul 31 1987
Externally publishedYes

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Vitamin D-Binding Protein
Conformations
Actins
Tissue
Extracellular Space
Isoelectric Focusing
Necrosis
Fluorescence
Serum
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Altered conformation of Gc (Vitamin D-binding protein) upon complexing with cellular actin. / Goldschmidt-Clermont, Pascal; Williams, Merfyn H.; Galbraith, Robert M.

In: Biochemical and Biophysical Research Communications, Vol. 146, No. 2, 31.07.1987, p. 611-617.

Research output: Contribution to journalArticle

Goldschmidt-Clermont, Pascal ; Williams, Merfyn H. ; Galbraith, Robert M. / Altered conformation of Gc (Vitamin D-binding protein) upon complexing with cellular actin. In: Biochemical and Biophysical Research Communications. 1987 ; Vol. 146, No. 2. pp. 611-617.
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