Skip to main content
SpringerLink
Log in

Analysis of colloidal gold methods for labelling proteins

  • Published:
Histochemistry Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Ackerman GA, Wolken KW, Gelder FB (1980) Different expression of surface monosialogan glioside GMI in various hemic cell lines of normal human bone marrow. A quantitative immunocytochemical study using the cholera toxin-gold-labelled anti-cholera toxin procedure. J Histochem Cytochem 28:1334–1342

    Google Scholar 

  • Batten TFC, Hopkins CR (1979) Use of protein A-coated colloidal gold particles for immuno-electromicroscopic localization of ACTH on ultrathin sections. Histochemistry 60:317–320

    Google Scholar 

  • Bendayan M (1981) Use of the protein A-gold technique for the morphological study of vascular permeability. J Histochem Cytochem 28:1251–1254

    Google Scholar 

  • Bendayan M (1981) Ultrastructural localization of nucleic acids by the use of enzyme-gold complexes. J Histochem Cytochem 29:531–541

    Google Scholar 

  • Frens G (1972) Particle size and sol stability in metal colloids. Kollid Z Z Polym 250:736–741

    Google Scholar 

  • Frens G (1973) Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nature (Phys Sci) 241:20–22

    Google Scholar 

  • Geoghegan WD, Ackerman AG (1977) Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin in colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: a new method, theory and application. J Histochem Cytochem 25:1187–1200

    Google Scholar 

  • Geoghegan WD, Scillian JJ, Ackerman GA (1978) The detection of human B lymphocytes by both light and electron microscopy utilizing collidal gold labeled anti-immunoglobulin. Immunol Commun 7:1–12

    Google Scholar 

  • Geoghegan WD, Ambegaonka S, Calvanico NJ (1980) Passive gold agglutination. An alternative to passive hemagglutination. J Immunol Methods 34:11–21

    Google Scholar 

  • Horisberger M, Rosset J, Bauer H (1975) Colloidal gold granules as markers for cell surface receptors in the scanning electron microscope. Experientia 31:1147–1149

    Google Scholar 

  • Horisberger M, Rosset J (1977) Colloidal gold, a useful marker for transmission and scanning electron microscopy. J Histochem Cytochem 25:295–305

    Google Scholar 

  • Horisberger M, Rosset J, Vonlanthen M (1978) location of lectin receptors on rat hepatocytes by transmission and scanning electron microscopy. Experientia 34:274–276

    Google Scholar 

  • Horisberger M, Vonlanthen M (1978) Simultaneous localization of an hepatic binding protein specific for galactose and of galactose-containing receptors on rat hepatocytes. J Histochem Cytochem 26:960–966

    Google Scholar 

  • Horisberger M, Vonlanthen M (1979) Multiple marking of cell surface receptors by gold granules: simultaneous localization of three lectin receptors on human erythrocytes. J Microse 115:97–102

    Google Scholar 

  • Larsson L-I (1979) Simultaneous ultrastructural demonstration of multiple peptides in endocrine cells by a novel immunocytochemical method. Nature 282:743–746

    Google Scholar 

  • Mace ML Jr, Van NT, Conn MP (1977) Electron microscopic localization of DNA-dependent RNA polymerase binding sites on DNA using enzyme immobilized on colloidal gold. Cell Biol Rep 1:527–533

    Google Scholar 

  • Roth J, Wagner M (1977) Peroxidase and gold complexes of lectins for double labeling of surface-binding sites by electron microscopy. J Histochem Cytochem 25:1181–1184

    Google Scholar 

  • Roth J, Bendayan M, Orci L (1978) Ultrastructural localization of intracellular antigens by the use of protein A-gold complex. J Histochem Cytochem 26:1074–1081

    Google Scholar 

  • Roth J, Binder M (1978) Colloidal gold, ferritin and peroxidase as markers for electron microscopic double labeling lectin techniques. J Histochem Cytochem 26:163–169

    Google Scholar 

  • Roth J, Bendayan M, Orci L (1980) FITC-protein A-gold complex for light and electron microscopic immunocytochemistry. J Histochem Cytochem 28:55–57

    Google Scholar 

  • Roth J, Ravazzola M, Bendayan M, Orci L (1981) Application of the protein A-gold technique for electron microscopic demonstration of polypeptide hormones. Endocrinology 108:247–253

    Google Scholar 

  • Scatchard G (1976) Surface and colloid chemistry. Harvard University Press, Cambridge, pp 213–279

    Google Scholar 

  • Williams VR, Williams HB (1973) Bsic physical chemistry for the life sciences. WH Freeman, San Francisco, pp 328–341

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Histology and Embryology, Institute of Biostructure, Medical Academy of Poznan, Swiecickiego 6, Poznan, Poland

    J. B. Warchol & R. Brelińska (Recipients of a Humboldt Fellowship from the Federal Republic of Germay)

  2. Department of Anatomy, The University of Texas, Health Science Center at San Antonio, 78284, San Antonio, Texas, USA

    D. C. Herbert

  3. Department of Clinical Morphology, University of Ulm, Oberer Eselsberg, D-7900, Ulm/Donau, Federal Republic of Germany

    J. B. Warchol & R. Brelińska (Recipients of a Humboldt Fellowship from the Federal Republic of Germay)

Authors
  1. J. B. Warchol
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. R. Brelińska
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. D. C. Herbert
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Warchol, J.B., Brelińska, R. & Herbert, D.C. Analysis of colloidal gold methods for labelling proteins. Histochemistry 76, 567–575 (1982). https://doi.org/10.1007/BF00489911

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00489911

Keywords

Search

Navigation