Production of lysozyme and lysozyme-superoxide dismutase dimers bound by a ditryptophan cross-link in carbonate radical-treated lysozyme
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- 作者：Verô ; nica Paviania ; Raphael F. Queirozb ; Emerson F. Marquesa ; Paolo Di Mascioa ; Ohara Augustoa ; oaugusto@iq.usp.br" class="auth_mail" title="E-mail the corresponding author
- 关键词：CoC ; carbonatotetrammine cobalt(III) complex ; DMPO ; 5 ; 5-dimethylpyrroline-N-oxide ; DTPA ; diethylenetriamine-N ; N ; N´ ; N´ ; -pentaacetic acid ; hSOD1 ; human superoxide dismutase 1 ; Lyso ; lysozyme ; MNP ; 2-methyl-2-nitrosopropane
- 刊名：Free Radical Biology and Medicine
- 出版年：2015
- 出版时间：December 2015
- 年：2015
- 卷：89
- 期：Complete
- 页码：72-82
- 全文大小：1625 K
文摘
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Lysozyme (Lyso) was oxidized by photolytically- or hSOD1-generated carbonate radical.
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Oxidation resulted in Lyso inactivation and covalent dimerization.
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Lyso monomer was oxidized at Trp28,62 and 123 by photolysis and at Trp28 by hSOD1.
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Lyso and Lyso-hSOD1 dimers bound by a ditryptophan cross-link were characterized by MS.
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The tendency of the carbonate radical to promote cross-links is confirmed.