Purification and Properties of Neurospora crassa Laccase
AUTOR(ES)
Froehner, Stanley C.
RESUMO
Extracellular Neurospora laccase (p-diphenol:oxygen oxidoreductase; EC 1.10.3.2) has been purified to apparent homogeneity by classical purification techniques. The enzyme, which consists of mainly one form, has a molecular weight of 64,800 and contains 11% carbohydrate. The ultraviolet, visible, and electron paramagnetic resonance spectra indicate that both type I and type II copper are present, as described for the Polyporus versicolor enzyme. With the exception of phloroglucinol, only para- and ortho-diphenols serve as effective substrates for the enzyme. Like the extracellular form, intracellular laccase is a glycoprotein as shown by its ability to bind to Concanavalin A Sepharose. Other studies, including gel filtration and ion-exchange chromatography, revealed no differences between the intracellular and extracellular enzymes, suggesting that intracellular laccase is destined for excretion by the cell.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=245783Documentos Relacionados
- Purification and properties of DNA-dependent DNA-polymerases from Neurospora crassa.
- Isolation and characterization of a laccase-derepressed mutant of Neurospora crassa.
- Induction of Neurospora crassa Laccase with Protein Synthesis Inhibitors
- Purification of vacuoles from Neurospora crassa.
- Purification and properties of the fatty acids synthetase complex from Neurospora crassa, and the nature of the fas-mutation.
