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Abstract Human augmenter of liver regeneration protein (hALRp) had a fragment of Cys-Xaa-Xaa-Cys(CXXC) amino acid sequence. In order to study the CXXC activity motif ALRp, the amino acid at the position of 65 and 88 in hALRp was exchanged against alanine and cysteine respectively, and then expressed and purified mutagenesis protein. The sulfhydryl oxidase activity of ALRp and its mutagenesis in vitro were detected. The concentration of thiol groups in ALR-FAD and ALRQ88C-FAD group were decreased, and they had significant difference when contrasted to control (P<0.05), but ALRC65AFAD group had no significant difference when contrasted to control. The mutation of C65A that changed the CXXC motif of hALRp deprived all of its activity of sulfhydryl oxidase. The mutation of Q88C that added another CXXC motif in hALR couldn’t improve its activity of sulfhydryl oxidase. At the same time, FAD was a cofactor that was indispensable to the activity of sulfhydryl oxidase of ALR, and it maybe helps the mutation protein at the time of renaturation.
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Received: 08 February 2006
Published: 25 February 2006
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