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Applied Microbiology and Biotechnology

, Volume 56, Issue 3–4, pp 402–405 | Cite as

Isolation and characterization of a cell-associated protein of Bacillus pumilus PH-01

  •  H.-B. Hong
  •  Y.-S. Chang
  •  S.-D. Choi
  •  I.-H. Nam
  •  Y.-E. Lee
Original Paper

Abstract.

A cell-associated protein released from Bacillus pumilus PH-01 showed an affinity for some dioxins, like 1,2,3,4-tetrachlorodibenzo-p-dioxin (TCDD) and 1,2,3,4-tetrachlorodibenzofuran (TCDF), and the concentration of the protein increased when B. pumilus PH-01 was boiled in minimal salts medium. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and matrix-assisted laser desorption ionization-mass spectrometry revealed that the boiled culture supernatant contained a major protein with a molecular mass of 5,313.4 Da. The adsorption behavior of the protein for 1,2,3,4-TCDD and 1,2,3,4-TCDF was examined by digesting it with proteinase K and trypsin, showing that the proteolyzed protein lost the ability to adsorb the compounds. The amino acid sequence of the protein was determined by automated Edman degradation and tandem mass spectrometry. A search of the protein databases showed no existence of proteins with an homologous sequence.

Keywords

Tandem Mass Spectrometry Dioxin TCDD Laser Desorption Adsorption Behavior 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  •  H.-B. Hong
    • 1
  •  Y.-S. Chang
    • 1
  •  S.-D. Choi
    • 1
  •  I.-H. Nam
    • 1
  •  Y.-E. Lee
    • 2
  1. 1.School of Environmental Engineering, Pohang University of Science and Technology, San 31, Hyo-Ja dong, Nam-gu, Pohang 790-784, Korea
  2. 2.Department of Biochemistry, Dongguk University, Kyungju 780–714, Korea

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