Expression and secretion of recombinant aspartic proteinases by Bacillus brevis.
Hayashi
T
T
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Inoue
H
H
Kato
M
M
Udaka
S
S
Takahashi
K
K
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000096:biosynthesis* / Q000302:isolation & purification; D001234:Aspergillus niger / Q000201:enzymology / Q000235:genetics; D001407:Bacillus; D001483:Base Sequence; D003001:Cloning, Molecular / Q000379:methods*; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D005800:Genes, Fungal; D015151:Immunoblotting; D007700:Kinetics; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000302:isolation & purification; D029701:Saccharomyces cerevisiae Proteins
D016282:Aspartic Acid Endopeptidases; D017931:DNA Primers; D004792:Enzyme Precursors; D011994:Recombinant Proteins; D012697:Serine Endopeptidases; C023302:yeast proteinase B; D029701:Saccharomyces cerevisiae Proteins