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Fluorogenic Substrates Containing 7‐Amino‐4‐methyl‐2‐quinolinone for Aminopeptidase M, Chymotrypsin, Elastase and Trypsin, Determination of Enzyme Activity
Author(s) -
Tzougraki Chryssa,
Noula Catherine,
Geiger Reinhard,
Kokotos George
Publication year - 1994
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.199419940409
Subject(s) - chemistry , chymotrypsin , aminopeptidase , trypsin , elastase , enzyme , biochemistry , stereochemistry , amino acid , leucine
Several new fluorogenic substrates for four proteases were synthesized by coupling the highly fluorescent 7 ‐amino‐4‐methyl‐2‐quinolinone (AMeq) with appropriate amino acids and peptides. Compounds HCl · H‐Ala‐NH‐Meq ( 1 ) and HCl · H‐Leu‐NH‐Meq ( 2 ) are substrates for aminopeptidase M, Glt‐Tyr‐NH‐Meq ( 3 ) and Glt‐Leu‐Tyr‐NH‐Meq ( 4 ) for chymotrypsin, Boc‐(Ala) 4 ‐NH‐Meq ( 5 ) for elastase and Z‐Arg‐NH‐Meq ( 6 ) for trypsin. The kinetic parameters for the hydrolysis of the new substrates were determined and showed that each new substrate is suitable for a convenient fluorometric assay of the corresponding enzyme.