| Autor: |
MIYAMOTO, Takahisa, SAYED, Md. Abu, SASAHARA, Ryo, SUKIMOTO, Kouji, UMEZAKI, Akiko, HONJOH, Ken-ichi, IIO, Masayaoshi, HATANO, Shoji |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2002, Vol. 66 Issue: 1 p44-50, 7p |
| Abstrakt: |
The pbp3gene encoding PBP3 of Bacillus cereuswas cloned and sequenced. For this purpose, PBP3 was first purified from B. cereusts-4, and N-terminal amino acid sequences of the peptides obtained from the protease digests of the protein were analyzed. The B. cereusts-4 pbp3gene consisted of an open reading frame of 1,986 bp encoding 662 amino acid residues with a calculated molecular mass of 73,044 Da. The active site-motifs SXXK, SXN, and KTG are present at the positions 393, 452, and 590, respectively, in the deduced amino acid sequence. The pbp3structural gene was ligated into the pET17×b expression vector and pET-pbp3was constructed. A protein was produced by the cells of E. colicarrying pET-pbp3. The produced protein migrated at about 75 kDa in SDS-polyacrylamide gel and strongly reacted with biotinylated ampicillin. |
| Databáze: |
Supplemental Index |
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