Analysis of colloidal gold methods for labelling proteins

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...

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Bibliographic Details
Published in:Histochemistry 1982-01, Vol.76 (4), p.567-575
Main Authors: Warchol, J B, Brelińska, R, Herbert, D C
Format: Article
Language:English
Subjects:
Animals
Cattle
Colloids
Gold
Protein Binding
Proteins - analysis
Rabbits - immunology
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Summary: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.
ISSN:0301-5564
1432-119X
DOI:10.1007/BF00489911