1992 Volume 56 Issue 6 Pages 906-912
We have cloned the xynA gene coding for xylanase A, a major commponent of the xylanase family, from Aspergillus kawachii. The cDNA was isolated from an A.kawachii cDNA library by immunoscreening using antibody raised against the purified xylanase A protein. Nucleotide sequence analysis of the cDNA showed a 981-bp open reading frame that encoded a protein of 327 amino acid residues. The signal peptide was composed of 25 amino acid residues and the N-terminus of the mature protein was pyroglutamic acid. The transformed yeast with a cloned cDNA prodcued xylanase. The genomic DNA was arranged as ten exons and nine introns.
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