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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Interaction between a Blood Vessel-Inducing Protein Angiogenin and Its Binding Protein Actin

  • Chang, Soo-Ik (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • Paik, Seung-Bum (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • So, Seung-Ho (Department of Biochemistry, College of Natural Sciences. Chungbuk National University) ;
  • Ahn, Byung-Cheol (Department of Biochemistry, College of Natural Sciences. Chungbuk National University)
  • Received : 1996.03.08
  • Published : 1996.07.31
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Abstract

Bovine angiogenin (bAng) is a potent blood vessel inducing protein purified from cow In ilk. fluorescence spectroscopy has been used to study the interaction of bAng with actin in 50 mM Tris-HCl pH 7.5, and 1 mM $CaCl_2$ at $25^{\circ}C$. Actin contains four tryptophans but bAng contains no tryptophans. A 50% decrease in intrinsic fluorescence accompanied formation of the bAng/actin complex. By contrast, the interaction of RNase A, a homologous protein to bAng, with actin results in about 10% quenching of the fluorescence. Fluorescence titration experiments were performed by adding increasing concentrations of bAng (0~1.0 ${\mu}M$) to a constant concentration of actin (0.1 ${\mu}M$), and the dissociation constant $K_d$ for the bAng/actin complex and the stoichiometry n were measured as $20{\pm}1$ nM and $1.0{\pm}0.1$ respectively. These results suggest that the interaction between bAng with actin is specific and that quenching of actin fluorescence has occurred in the bAng/actin complex. The bAng binding sites of actin are discussed in the results of this study, and we propose that Trp-80 in the small domain of bovine actin is responsible for the bAng/actin binding.

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