The radiolysis of glyceraldehyde-3-phosphate dehydrogenase.
The yields in molecules per 100 eV for active-site and sulphydryl loss from glyceraldehyde-3-phosphate dehydrogenase have been determined in nitrous-oxide-saturated, aerated and argon-saturated solutions. Molecular hydrogen peroxide produces a sulphenic acid product, which can be repaired by post-irradiation treatment with dithiothreitol. Comparison of the yields under various conditions showed that in aerated solutions both .OH and .O2-radicals inactivated the enzyme with an efficiency of about 26 per cent. However, the efficiency of .OH in air-free solutions was less, and inactivation by .H and eaq- did not appear to be appreciable. There is a correlation between SH loss and loss of active sites.
D000388:Air; D001128:Argon; D003037:Cobalt Radioisotopes; D005720:Gamma Rays; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000528:radiation effects*; D009243:NAD; D009609:Nitrous Oxide; D013438:Sulfhydryl Compounds / Q000528:radiation effects
D003037:Cobalt Radioisotopes; D013438:Sulfhydryl Compounds; D009243:NAD; D001128:Argon; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D009609:Nitrous Oxide