THE MECHANISM OF ACTION OF AET. II. THE INTERACTION BETWEEN PROTEINS AND 2- MERCAPTOETHYLGUANIDINE AND BIS(2-GUANIDOETHYL) DISULFIDE IN AQUEOUS BUFFERED SOLUTIONS
The binding of 2-mercaptoethylguanidine (MEG) and the effects of gamma radiation of aqueous solutions of 2-mercaptoethylguanidine-C/sup 14/ (MEG-C/sup 14/ and bis(2-guanido-C/sup 14/-ethyl) disulfide (GED-C/sup 14/), or 2 mercapto-S/ sup 35/-ethylguanidine (MEG-S/sup 35/) and bis(2-guanidoethyl) disulfide-S/sup 35/ (GED-S/sup 35/ and proteins are discussed. The radioactive species present before and after irradiation of aqueous buffered solutions of MEG-C/sup 14/ and GED-C/sup 14/, or MEG-S/sup 35/ and GED-S/sup 3/< s5>s and proteins were identified by means of paper strip chromatography and paper electrophoresis. The proteinMEG-C/sup 14/ complexes formed were isolated both by dialysis and by passage through a column of Sephadex. In solution, the complexes were cleared by the addition of thiols and disulfides. Guanidine, ethylamine, and tuurocyamine also displace a small amount of MEG from the complex. Irradiation of aqueous, buffered solutions of MEG and GED containing high protein concentration produced no detectable oxidation product of GED. The amount of protein-bound MEG increased considerably. Cleavage of irradiated complexes was more difficult than cleavage of the nonirradiated complex. (M.C.G.)
- Research Organization:
- Albert Einstein Medical Center, Philadelphia
- Sponsoring Organization:
- USDOE
- NSA Number:
- NSA-15-012789
- OSTI ID:
- 4075101
- Journal Information:
- Radiation Research, Journal Name: Radiation Research Vol. Vol: 14
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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