Analysis of colloidal gold methods for labelling proteins

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

doi:10.1007/BF00489911

Analysis of colloidal gold methods for labelling proteins

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

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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 language	English (US)
Pages (from-to)	567-575
Number of pages	9
Journal	Histochemistry
Volume	76
Issue number	4
DOIs	https://doi.org/10.1007/BF00489911
State	Published - Dec 1982
Externally published	Yes

ASJC Scopus subject areas

Anatomy
Agricultural and Biological Sciences(all)

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title = "Analysis of colloidal gold methods for labelling proteins",

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.",

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year = "1982",

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AB - 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.

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Analysis of colloidal gold methods for labelling proteins

Abstract

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