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Radiation effects on the native structure of proteins: fragmentation without dissociation.

作者信息

Miller J H, Fedoronko D A, Hass B D, Myint M, Kempner E S

机构信息

Laboratory of Physical Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.

出版信息

Arch Biochem Biophys. 1998 Apr 15;352(2):281-7. doi: 10.1006/abbi.1998.0604.

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.

摘要

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