Identification of a silver binding protein associated with the cytological silver staining of actively transcribing nucleolar regions.
Nucleoli isolated from Novikoff hepatoma cells were stained with AgNO3 to demonstrate the typical staining of active ribosomal cistrons. Pre-treatment of the nucleoli with 80 mM Tris-HCl (pH 7.5) -- 2.0 M NaCl did not interfere with silver staining. Treatment of the nucleoli with 80 mM Tris-HCl (pH 7.5) -- 0.15 M NaCl did, however, eliminate silver binding. Serial extraction of nucleoli with 2.0 M NaCl buffer followed by 0.15 M NaCl buffer also abolished silver staining. Analysis of the supernatant fraction of these extracts by polyacrylamide gel electrophoresis indicates that, although more than one nucleolar protein can bind silver, only one protein is associated with the staining of active ribosomal cistrons.
D000818:Animals; D002466:Cell Nucleolus / Q000187:drug effects / Q000378:metabolism*; D005260:Female; D008114:Liver Neoplasms, Experimental / Q000648:ultrastructure*; D009363:Neoplasm Proteins / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D012834:Silver / Q000378:metabolism*; D012835:Silver Nitrate; D012965:Sodium Chloride / Q000494:pharmacology; D013194:Staining and Labeling / Q000379:methods*
D009363:Neoplasm Proteins; D009698:Nucleoproteins; D012834:Silver; D012965:Sodium Chloride; D012835:Silver Nitrate