Purification and Properties of Novel Calcium-binding Proteins from Streptomyces coelicolor

  • Chang, Ji-Hun (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
  • Yoon, Soon-Sang (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
  • Lhee, Sang-Moon (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
  • Park, I-Ha (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
  • Jung, Do-Young (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
  • Park, Young-Sik (Department of Microbiology, Inje University) ;
  • Yim, Jeong-Bin (Department of Microbiology, College of Natural Sciences, Seoul National University)
  • Published : 1999.03.01

Abstract

Two novel calcium-binding proteins, named CAB-I and CAB-II, have been isolated from Streptomyces coelicolor. Purification of the calcium-binding proteins involved heat treatment, fractionation with ammonium sulfate, acid treatment, anion exchange and hydrophobic interaction column chromatography, FPLC gel filtration, and preparative isoelectric focusing. A chelex competitive assay and 45Ca autoradiography verified the calcium-binding ability of the proteins. The major band CAB-II has an apparent molecular weight of 26,000 determined by SDS-polyacrylamide gel electrophoresis and 340,000 determined by gel filtration. The isoelectric point of this molecule showed the acidic nature of the molecule. N-terminal amino acid sequence analysis shows homology to rat Ca2+/calmodulin-dependent protein kinase-II (CAB-II) and yeast phosphoprotein phosphatase (CAB-I).

Keywords

References

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