Journal of the Korean Chemical Society (대한화학회지)

Korean Chemical Society (대한화학회)
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Pepsin Action on the New Synthetic Peptides 1. Pepsin action on benzyloxycarbonyl-glycyl-L-tyrosyl-L-phenylalanyl-glycine and its ethyl ester

새로운 합성 펩티드에 대한 펩신 작용 1. Benzyloxycarbonyl-glycyl-L-tyrosyl-L-phenylalanyl-glycine 과 그의 에틸에스테르에 대한 펩신 작용

  • Yoon, Joo-Ok (Dept. of Food Tech., College of Industry, Dongguk Univ.) ;
  • Shin, Hong-Dae (Dept. of Food Tech., College of Industry, Dongguk Univ.)
  • 윤주억 (동국대학교 산업대학 식품공학과) ;
  • 신홍대 (동국대학교 산업대학 식품공학과)
  • Published : 19690900
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Abstract

The synthesis is described of new pepsin substrates of benzyloxycarbonyl-glycyl-L-tyrosyl-L-phenylalanyl-glycine ethyl ester and benzyloxycarbonyl-glycyl-L-tyrosyl-L-phenylalanyl-glycine for studies on the specificity of pepsin, and thin layer chromatographic examination of the peptides prepared showed the new substrates are homogeneous and also, same examination of the incubation mixtures showed that two synthetic substrates are cleaved by pepsin at the L-tyrosyl-L-phenylalanyl bond and hydrolysis of these substrates by pepsin is achieved without transpeptidation. It is found that synthetic peptides are moderately soluble with the amount of the substrate up to a concentration of 0.7 mM in aqueous sodium citrate buffers (0.04 M) in the pH range 1.8-4.0, thus obviating the necessity for the adding of an organic solvent in the assay mixture. The kinetic parameters for synthetic substrates are tabulated in the following table. The data in the table indicate that the susceptibility of synthetic peptides to peptic hydrolysis are relatively large and the change of the carboxyl-terminal group of synthetic substrate from glycine ethyl ester to glycine causes a small decrease in the susceptibility of the L-tyrosyl-L-phenylalanyl bond.

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References

  1. Biochem. J. v.73 H. Neumann;Y. Levin;A. Berger;E. Katchalski
  2. J. Biol. Chem. v.240 J. Tang
  3. J. Am. Chem. Soc. v.87 M. S. Silver;J. L. Denburg;J. J. Steffens
  4. J. Am. Chem. Soc. v.88 E. Zeffren;E. T. Kaiser
  5. J. Am. Chem. Soc. v.89 E. Zeffren;E. T. Kaiser
  6. Chem. of the Amino Acids v.II J. P. Greenstein;M. Winitz
  7. J. Chem. Soc., Japan v.83 T. Kato;S. Makisumi;M. Ohno;N. Izumiya
  8. J. Am. Chem. Soc. v.74 J. R. Vaughan, Jr.;R. L. Osato
  9. J. Biochem., Japan v.46 N. Izumiya;H. Uchio
  10. J. Am. Chem. Soc. v.82 K. Hofmann;T. A. Thompson;M. E. Woolner;G. Spuhler;H. Yajima;J. D. Cipera;E. T. Schwartz
  11. Helv. Chim. Acta. v.38 R. A. Boissonnas;St. Guttmann;P. A. Jaquenoud;J. P. Waller
  12. Helv. Chim. Acta. v.43 R. Schwyzer;P. Sieber
  13. J. Biol. Chem. v.193 L. E. Baker
  14. Biochemistry v.5 K. Inouye;I. M. Voynick;G. R. Delpierre;J. S. Fruton
  15. Introduction to Enz. Chem. K. Nisizawa;K. Shimura
  16. J. Biol. Chem. v.56 H. Lineweaver;D. Burk
  17. J. Theoret. Biol. v.9 J. R. Knowles
  18. Ann. Rev. Biochem v.34 M. L. Bender;F. J. Kezdy
  19. Nature v.199 J. Tang