On the reconstitution of laccase from the chinese lacquer tree

Hauenstein, Bennett L.; McMillin, David R.

doi:10.1016/s0006-291x(78)80070-9

Cited by 6 publications

(2 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In one case, apoprotein was produced under low copper levels (Bligny et al, 1986), but the activity could not be reconstituted by incubation with copper. On the other hand, reconstitution of laccase from the Chinese lacquer tree requires the addition of Cu(I) and not Cu(II) (Hauenstein & McMillin, 1978). Omura (1961) also reported that Cu(I), but not Cu(II), could be used to reconstitute the apoprotein, results that were confirmed by Ando (1970).…”

Section: Discussionmentioning

confidence: 95%

Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns

et al. 2003

View full text Add to dashboard Cite

Analysis of genomic clones encoding a putative laccase in homokaryon strains of Ceriporiopsis subvermispora led to the identification of an allelic variant of the previously described lcs-1 gene. A cDNA clone corresponding to this gene was expressed in Aspergillus nidulans and in Aspergillus niger. Enzyme assays and Western blots showed that both hosts secreted active laccase. Relative to the isozymic forms of the native C. subvermispora enzyme, the A. niger-produced laccase had a higher molecular mass and gave a single band on IEF gels. In contrast, A. nidulans transformants secreted several isoforms remarkably similar to those of the native system. Considered together with previously reported Southern blots and protein sequencing, expression in A. nidulans supports the view that C. subvermispora has a single laccase gene and that multiple isoforms result from post-translational processes. In addition, several lines of evidence strongly suggest that under copper limitation, A. nidulans secretes apoprotein which can be reconstituted by a short incubation with Cu(I) and to a lesser extent with Cu(II).

show abstract

Section: Discussionmentioning

confidence: 95%

Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Apostellacyanin (Morpurgo et al, 1972) and apolaccase were prepared and reconstituted by anaerobic incubation with cuprous chloride in excess sodium chloride (Hauenstein et al, 1978) for 4-5 days, followed by exhaustive dialysis against Tris [tris(hydroxymethyl)aminomethane] buffer (25 mM, pH 7.4, for lacease and 50 mM, pH 8.2, for stellacyanin). Isotopic CuCl was prepared by dissolution in HC1 of 63Cu20 and 65Cu20, prepared (Parker, 1964) from the corresponding curpic oxides (99.9% 63Cu and 99.7% 65Cu, Oak Ridge National Laboratories).…”

Section: Methodsmentioning

confidence: 99%