The Binding of Radioprotective AET to Proteins
- 1 January 1972
- journal article
- research article
- Published by Taylor & Francis in International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine
- Vol. 21 (3) , 263-278
- https://doi.org/10.1080/09553007214550301
Abstract
Among the -SH radioprotectors, AET has been the subject of many investigations but little work has been done on -SH group-containing, biologically-active proteins that might enter exchange reactions forming mixed disulphides. In this investigation in vitro experiments were performed to reveal the mechanism of mixed disulphide formation. Physico-chemical changes, such as absorption spectra, electrophoretic mobility and polarographic behaviour of biologically-active proteins such as insulin and oxyhaemoglobin were examined as well as changes in biological activity.Keywords
This publication has 4 references indexed in Scilit:
- Hydrolysis of disulfide bonds in weakly alkaline media. I. Oxidized glutathioneBiochimica et Biophysica Acta (BBA) - General Subjects, 1969
- The heterogeneity of bovine serum albuminBiochimica et Biophysica Acta (BBA) - General Subjects, 1966
- DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINSProceedings of the National Academy of Sciences, 1965
- The association of insulin molecular units in aqueous solutionsArchives of Biochemistry and Biophysics, 1956