BMB Reports
- 제32권3호
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- Pages.239-246
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- 1999
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- 1976-670X(eISSN)
The Purification and Characterization of Bacillus subtilis Tripeptidase (PepT)
- Park, Yong-Seek (Department of Biochemistry and Molecular Biology, Hanyang University) ;
- Cha, Myung-Hoon (Department of Biochemistry and Molecular Biology, Hanyang University) ;
- Yong, Whan-Mi (Department of Biochemistry and Molecular Biology, Hanyang University) ;
- Kim, Hyo-Joon (Department of Biochemistry and Molecular Biology, Hanyang University) ;
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Chung, Il-Yup
(Department of Biochemistry and Molecular Biology, Hanyang University) ;
- Lee, Young-Seek (Department of Biochemistry and Molecular Biology, Hanyang University)
- 투고 : 1998.11.18
- 심사 : 1998.12.29
- 발행 : 1999.05.31
초록
A tripeptidase (PepT) was purified to homogeneity from Bacillus subtilis through four sequential chromatographies including DEAE-Sepharose ion exchange, hydroxylapatite, mono-Q FPLC ion exchange, and Superose-12 FPLC gel filtration. The apparent molecular mass of the enzyme was 49,200 Da and 51,400 Da as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography, respectively, and the enzyme exists in a monomeric form. The physicochemical properties of the enzyme were as follows: optimum pH at 7.5, optimum temperature at