Preparation of protein colloidal gold complexes in the presence of commonly used buffers.

Abstract:

:In the presence of various commonly used buffers, phosphate-buffered saline (PBS), tris-buffered saline (TBS), Na-cacodylate, bovine serum albumin and a wide range of cytochemically active proteins (monoclonal and polyclonal IgG, concanavalin A, Ricinus communis lectin I, Helix pomatia lectin, protein A) were complexed to colloidal gold of different particle sizes (6 nm, 9 nm, 22 nm). The resulting complexes were active in cytochemical labelling. Complex-formation in the presence of electrolyte opens the possibilities of: maintenance of ionic environment during complexing of proteins sensitive to low ionic strength, pH control by addition of buffers to the protein solution or to the gold sol, direct coupling of protein supplied in PBS or saline avoiding dialysis against low ionic strength buffers. Using the electron microscope to estimate the protein amounts needed for stabilization provided a sensitive and economical method to obtain aggregate-free protein-gold complexes.

journal_name

Eur J Cell Biol

authors

Lucocq JM,Baschong W

subject

Has Abstract

pub_date

1986-12-01 00:00:00

pages

332-7

issue

2

eissn

0171-9335

issn

1618-1298

journal_volume

42

pub_type

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