| Literature DB >> 8835340 |
N Do Nascimento1, C S Seebart, B Francis, J R Rogero, I I Kaiser.
Abstract
Irradiation of crotoxin and its subunits with 2000 Gy of gamma-rays from 60Co source leads to aggregation and generation of lower mol. wt breakdown products. Aggregates separated by gel filtration retain at least part of their higher-ordered structure, based on their reactivity with monoclonal antibodies known to react with conformational epitopes in native crotoxin. These same aggregates can serve as antigens to raise antisera that cross-react and neutralize crotoxin. Compared with native crotoxin, aggregates appear less myotoxic, are largely devoid of phospholipase activity, and are virtually non-toxic in mice. These results indicate that irradiation of toxic proteins can promote significant detoxification, but still retain many of the original antigenic and immunological properties of native crotoxin.Entities:
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Year: 1996 PMID: 8835340 DOI: 10.1016/0041-0101(95)00111-5
Source DB: PubMed Journal: Toxicon ISSN: 0041-0101 Impact factor: 3.033