Characterization of the Binding Activity of Virginiae Butanolide C Binding Protein in Streptomyces virginiae

Streptomyces virginiae가 생산하는 Virginiae Butanolide C(VB-C) 결합단백질의 결합활성에 미치는 일반적 특성

  • 김현수 (계명대학교 자연과학대학 미생물학과)
  • Published : 1992.06.01


Virginiae butanolide (VB) is an autoregulator which triggers virginiamycin production in Strefltomyces virginiae. VB-C binding protein activity was investigated under various additives. The VB-C binding protein was almost fully observed in sotubte fraction (>90%) and the binding activity was optimum at pH 7.0. The VB-C binding activity was increased about 15% in 0.5 M KCI, whereas decreased about 60% in 20 mM $Mo^{6+}$. Chelating reagents (ethylenediarnine tetraacetic acid, ethyleneglycol bis(2-aminoethylether) tetraacetic acid, 8-hydroxyquinoline) and SH protecting reagents (rnercaptoethanol, dithiothreitol, thioglycerol) inhibited the VB-C binding activity about 30~55% and 3~20%, respectively. Serine protease inhibitor (phenyl methane sulfonyl fluoride), nucleotides (guanosine 5'-monophosphate, adenosine 3',5'-cyclic monophosphate), and phosphatases (alkaline, acid phosphatase) increased the VB-C binding activity about 17%, 6~20%, and 4- 13%, respectively.


Streptomyces virginiae;virginiae butanolide C(VB-C);VB-C binding protein;bacterial hormone.