Radiation effects on the native structure of proteins: fragmentation without dissociation.
Several proteins (avidin, carboxypeptidase B, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, maltase, and peroxidase) composed of one to six subunits were irradiated in the frozen state. Each irradiated protein was examined by size-exclusion chromatography (SEC) and by denaturing gel electrophoresis (SDS-PAGE). All these proteins eluted from SEC as a single peak even though SDS-PAGE showed cleavage of the polypeptide backbone of the monomers. Thus, fragmentation of the subunits did not result in dissociation of the oligomeric structure.
Miller
J H
JH
Laboratory of Physical Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Fedoronko
D A
DA
Hass
B D
BD
Myint
M
M
Kempner
E S
ES
D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000737:chemistry / Q000528:radiation effects; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry / Q000528:radiation effects; D005969:Glutamate Dehydrogenase / Q000737:chemistry / Q000528:radiation effects; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry* / Q000528:radiation effects*; D000520:alpha-Glucosidases / Q000737:chemistry / Q000528:radiation effects
D011506:Proteins; D005954:Glucosephosphate Dehydrogenase; D005969:Glutamate Dehydrogenase; D000520:alpha-Glucosidases; D002268:Carboxypeptidases; D043424:Carboxypeptidase B