Analysis of colloidal gold methods for labelling proteins |
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| Authors: | J. B. Warchol R. Brelińska D. C. Herbert |
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| Affiliation: | (1) Department of Histology and Embryology, Institute of Biostructure, Medical Academy of Poznan, Swiecickiego 6, Poznan, Poland;(2) Department of Anatomy, The University of Texas, Health Science Center at San Antonio, 78284 San Antonio, Texas, USA;(3) Department of Clinical Morphology, University of Ulm, Oberer Eselsberg, D-7900 Ulm/Donau, Federal Republic of Germany |
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| Abstract: | 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. |
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