Studies on the synthesis of proteinase inhibitors. I. Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitor.

@article{Nishino1977StudiesOT,
  title={Studies on the synthesis of proteinase inhibitors. I. Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitor.},
  author={Norikazu Nishino and Haruhiko Aoyagi and Tomoki Kato and Naotaka Izumiya},
  journal={Journal of biochemistry},
  year={1977},
  volume={82 3},
  pages={901-9}
}
Two heterodetic cyclic nonapeptides, X-Cys-Thr-Lys-Ser-Asn-Pro-Pro-Gln-Cys-Y (Ia: X = Ac, Y = NH2; Ib: X = H, Y = OH), which correspond to residues 14-22 in the sequence of Bowman-Birk inhibitor, have been synthesized by Merrifield's solid-phase method. Inhibitory activities of Ia and Ib on tryptic hydrolysis of amide and ester substrates were examined. When Gly2-Lys-Gly3 and Tos-Arg-OMe were used as substrates, the values of I50 for the peptide Ia were calculated to be 3.6 micron and 40 micron… CONTINUE READING

From This Paper

Topics from this paper.

Similar Papers

Loading similar papers…