Fractionation of the ribosome inactivating protein preparations with triazine dyes.

Abstract

Aspergillins are ribosome-inactivating proteins (RIPs), isolated from several strains of Aspergillus. The interaction between Cibacron Blue F3GA and two members of this family, alpha sarcin and mitogillin, and other RIPs of type I, was studied. Alpha sarcin retention depended on pH and ionic strength. By chromatography on Affi-Gel Blue in mild experimental conditions, mitogillin and PAP-I did not interact with the dye, whereas 40% of alpha sarcin and 70-90% of briodin, RTA and gelonin were recovered in the bound fraction. In all cases, the major fraction showed a higher toxicity level in protein synthesis inhibition assays. The unbound alpha sarcin, conjugated with the anti-ovarian carcinoma monoclonal antibody MOv17, showed on OVCA 432 a cytotoxicity which was 900 times higher than that exerted by the alpha sarcin alone.

• Authors: S M Muñoz, M Caldera, S Canevari, E Tosi, T Cogliati, M I Colnaghi, F P Conde
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 173 Issue 2 Pg. 554-60 (Dec 14 1990) ISSN: 0006-291X [Print] United States
• PMID: 2260968 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies, Monoclonal
• Fungal Proteins
• Protein Synthesis Inhibitors
• Triazines
• alpha-sarcin
• Cibacron Blue F 3GA
• Endoribonucleases

Topics

• Antibodies, Monoclonal (immunology)
• Aspergillus (analysis)
• Cytotoxicity, Immunologic
• Endoribonucleases
• Fungal Proteins (isolation & purification, metabolism)
• Humans
• Hydrogen-Ion Concentration
• Protein Synthesis Inhibitors (pharmacology)
• Triazines
• Tumor Cells, Cultured (drug effects, immunology)