Molecular and enzymic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells

Biochemical Journal

Volumn 339, Issue 3, 1999, Pages 589-597

  Ichishima, Eiji ^a,b   Taya, Noriyuki ^a   Ikeguchi, Masamichi ^a   Chiba, Yasunori ^c   Nakamura, Motoyoshi ^b   Kawabata, Choko ^a,d   Inoue, Takashi ^b   Takahashi, Koji ^e   Minetoki, Toshiki ^f   Ozeki, Kenji ^f   Kumagai, Chieko ^f   Gomi, Katsuya ^b   Yoshida, Takashi ^b   Nakajima, Tasuku ^b  

^a SOKA UNIVERSITY   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c KIRIN BREWERY CO LTD   (Japan)

^d T Hasegawa Co   (Japan)

^e TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^f Ozeki Corporation   (Japan)

Author keywords

1,2 mannosidase; Aspergillus oryzae; Aspergillus saitoi; Overexpression; Recombinant mannosidase

Indexed keywords

ASPERGILLOPEPSIN; CALCIUM; MANNOSE; MANNOSIDASE; N ACETYLGLUCOSAMINE; PEPSIN A; PYRANOSIDE; RECOMBINANT ENZYME; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; ASPERGILLUS; ASPERGILLUS ORYZAE; ATOMIC ABSORPTION SPECTROMETRY; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; ENZYME ACTIVITY; ENZYME SPECIFICITY; GEL FILTRATION; GENE FUSION; GENE OVEREXPRESSION; GENETIC TRANSFORMATION; HYDROLYSIS; MELTING POINT; MOLECULAR WEIGHT; NONHUMAN; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SEQUENCE ANALYSIS; ULTRAVIOLET SPECTROSCOPY;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; ASPERGILLUS; ASPERGILLUS ORYZAE; CALCIUM; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; GENOME, FUNGAL; GLYCOSYLATION; ISOELECTRIC POINT; MANNOSE; MANNOSIDASES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OLIGOSACCHARIDES; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SPECTROPHOTOMETRY, ATOMIC; SUBSTRATE SPECIFICITY; TEMPERATURE; TRANSFORMATION, GENETIC;

ASPERGILLUS ORYZAE; ASPERGILLUS PHOENICIS; ASPERGILLUS SAITOI;

EID: 0033137074     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3390589     Document Type: Article

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