Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins.
Five intramolecularly quenched fluorogenic substrates for arginyl hydrolases with the sequence Abz-Phe-Arg-X-Y-EDDnp (X = Arg or Ser; Y = Val, Pro, or Arg) were synthesized by classical solution methods. Kinetics of their hydrolysis by tissue and plasma kallikreins, trypsin, and thrombin characterized Abz-Phe-Arg-Ser-Arg-EDDnp as a specific and sensitive substrate for the continuous assay of tissue kallikreins while Abz-Phe-Arg-Arg-Pro-EDDnp was the best substrate for human plasma kallikrein. The five peptides were poor substrates for trypsin and resistant to thrombin.
Chagas
J R
JR
Department of Biophysics, Escola Paulista de Medicina, Sao Paulo, Brazil.
Juliano
L
L
Prado
E S
ES
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006736:Horses; D006868:Hydrolysis; D007610:Kallikreins / Q000097:blood / Q000378:metabolism* / Q000652:urine; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism*; D010179:Pancreas / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
D009842:Oligopeptides; D007610:Kallikreins