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Arch Biochem Biophys ; 352(2): 281-7, 1998 Apr 15.
Article in English | MEDLINE | ID: mdl-9587417

ABSTRACT

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.


Subject(s)
Proteins/chemistry , Proteins/radiation effects , Carboxypeptidase B , Carboxypeptidases/chemistry , Carboxypeptidases/radiation effects , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Glucosephosphate Dehydrogenase/chemistry , Glucosephosphate Dehydrogenase/radiation effects , Glutamate Dehydrogenase/chemistry , Glutamate Dehydrogenase/radiation effects , Protein Conformation , Protein Denaturation , alpha-Glucosidases/chemistry , alpha-Glucosidases/radiation effects
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