Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/98902
Type: Artigo de periódico
Title: Dimethyl Sulfoxide As Chemical And Biological Probe: Conformational Effect On Peroxidase Systems
Author: Duran N.
Baeza J.
Freer J.
Brunet J.E.
Gonzalez G.A.
Sotomayor C.P.
Faljoni-Alario A.
Abstract: The variation of the spectra and its reactivity towards 2-methylpropanal, indole-3-acetic acid and malonaldehyde of solutions of horseradish peroxidase in dimethyl sulfoxide-water mixtures has been studied. A broad pattern of changes was observed in the CD spectra of peroxidase, especially in the 400 nm region. These variations influenced strongly the excited triplet acetone emission from the 2-methylpropanal system which is generated in the active site of the enzyme protected from external quenching. This means that presumably the active site is more uncovered in the presence of dimethyl sulfoxide than the native form. Energy transfer parameters indicate that in fact there is a conformational effect produced by dimethyl sulfoxide in the horseradish peroxide active site. Dimethyl sulfoxide appears to be an important conformational probe in biochemistry. © 1981.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/0006-291X(81)91670-3
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0019882961&partnerID=40&md5=f0bdb44f2606bb5e3a49cfa7b0ead686
Date Issue: 1981
Appears in Collections:Unicamp - Artigos e Outros Documentos

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