Protease, DNA encoding the same, and method for...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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Details

C530S300000, C435S069100, C435S006120, C435S320100, C435S325000, C435S252000

Reexamination Certificate

active

07601807

ABSTRACT:
A protease having the following characteristics:(i) a molecular weight of 21,000±1,000 (by SDS-PAGE) and(ii) specific protease activity cutting the Gly-Phe site of a peptide or protein comprising amino acid sequence (1) below, cutting the Gly-Phe site of a peptide or protein comprising amino acid sequence (2) below, or cutting the Ser-Leu site of a peptide or protein comprising amino acid sequence (3) below:(1) (SEQ ID NO:4)Pro-Gln-Gly-Phe-Gln-Gly-Pro(2) (SEQ ID NO:5)Pro-Ala-Gly-Phe-Ala-Gly-Pro(3) (SEQ ID NO:6)Gln-Thr-Gln-Ser-Leu-Val-Thr-Pro.DNA encoding this protease, including vectors containing this DNA, and a method for producing this protease by transforming a cell with this DNA.

REFERENCES:
patent: 07-067639 (1995-03-01), None
patent: 08-266276 (1996-10-01), None
patent: 2000-102381 (2000-04-01), None
patent: 2000-325095 (2000-11-01), None
patent: WO 2004/033668 (2004-04-01), None
Seffernick et al. (J. Bacteriology, vol. 183, pp. 2405-2410, 2001).
Wells, Biochemistry, vol. 29, pp. 8509-8517, 1990.
Lecroisey et al, FEBS Letters, (1975), vol. 59, No. 2, pp. 167-172.
Kabashima et al, Biochimica et Biophysica. Acta., (1999), vol. 1429, pp. 516-520.
Ogasawara et al, Biosci. Biotech. Biochem., (1997), vol. 61, No. 1, pp. 146-151.
Y. Kanayama, et al. “Purification and Properties of a New Type of Protease Produced by Microbacterium liquefaciens” Biosci. Biotechnol. Biochem., 69 (5), pp. 916-921, 2005.

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