Abstract:
:A cDNA coding for glucoamylase P of Hormoconis resinae was cloned using a synthetic oligonucleotide probe coding for a peptide fragment of the purified enzyme and polyclonal anti-glucoamylase antibodies. Nucleotide-sequence analysis revealed an open reading frame of 1848 base pairs coding for a protein of 616 amino-acid residues. Comparison with other fungal glucoamylase amino-acid sequences showed homologies of 37-48%. The glucoamylase cDNA, when introduced into Saccharomyces cerevisiae under the control of the yeast ADC1 promoter, directed the secretion of active glucoamylase P into the growth medium.
journal_name
Curr Genetjournal_title
Current geneticsauthors
Vainio AE,Torkkeli HT,Tuusa T,Aho SA,Fagerström BR,Korhola MPdoi
10.1007/BF00324663subject
Has Abstractpub_date
1993-07-01 00:00:00pages
38-44issue
1-2eissn
0172-8083issn
1432-0983journal_volume
24pub_type
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