Analysis of colloidal gold methods for labelling proteins

J. B. Warchol, R. Brelińska, D. C. Herbert

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

The relationship between unbound and bound proteins prepared during labelling with colloidal gold (Au) was investigated. For this aim, labelled 125I-bovine serum albumin and 125I-rabbit immunoglobulin were employed. The procedures associated with the washing of the Au labelled proteins (i.e. albumin) had a marked influence on the dissociation of the bound ligand. This was most evident when the concentration of albumin that was used for labelling was too high (0.1 or 1.0 mg/ml Au sol). We suggest that purification of labelled proteins be conducted shortly before use so as to avoid a significant amount of dissociation during the time when the solution is coming to equilibrium.

Original languageEnglish (US)
Pages (from-to)567-575
Number of pages9
JournalHistochemistry
Volume76
Issue number4
DOIs
StatePublished - Dec 1982
Externally publishedYes

ASJC Scopus subject areas

  • Anatomy
  • Agricultural and Biological Sciences(all)

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