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Tokunaga et al., 1992 - Google Patents

Characterization of Mouse α-Amylase Secreted from Saccharomyces cerevisiae by the pGKL 128 kDa Killer Secretion Signal

Tokunaga et al., 1992

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Document ID
14967595588572984188
Author
Tokunaga M
Kawamura A
Omori A
Hishinuma F
Publication year
Publication venue
Bioscience, biotechnology, and biochemistry

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Snippet

Amino-terminal amino acid sequences of glycosylated and non-glycosylated a.-amylases (SECRETED-AMY) were analyzed. For minor species, only two and five cycles of PTH- amino acids were identified because of their low contents. PREPROI28kDa-KIL and …
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • C12N9/6427Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
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    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
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