In:
European Journal of Biochemistry, Wiley, Vol. 235, No. 3 ( 1996-02), p. 508-515
Abstract:
A member of the laccase multigene family in Pleurotus ostreatus has been cloned and sequenced. The gene structure has been determined by comparison with the corresponding cDNA, synthesized by reverse transcription/PCR amplification. The gene encode a laccase isoenzyme of 533 amino acids which has already been purified and characterized [Palmieri, G., Giardina, P., Marzullo, L., Desiderio, B., Nitti, G., Cannio, R. & Sannia, G. (1993) Appl. Microbiol. Biotechnol. 39 , 632–636]. More than 92% of the protein sequence, including the N and C termini, has been verified by fast‐atom‐bombardment mass spectrometry, thus confirming the correspondence between the gene and its protein product. The protein was N‐glycosylated at Asn444. Glycan analysis showed the presence of only a high‐mannose structure containing varying numbers of mannose residues. The presence of O‐linked oligosaccharides as well as other post‐translational modification could be ruled out by the miss analysis.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1996.235.issue-3
DOI:
10.1111/j.1432-1033.1996.00508.x
Language:
English
Publisher:
Wiley
Publication Date:
1996
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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