Organic fluorescent reagents. XIV. Novel fluorogenic substrates for microdetermination of chymotrypsin and aminopeptidase: Bimane fluorescence appears after hydrolysis

Eisuke Sato, Mari Sakashita, Yuichi Kanaoka*, Edward M. Kosower

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The fluorescence of 9,10-dioxa-syn-3,4,6,7-tetramethylbimane (bimane) was found to be quenched in the presence of tryptophan or tyrosine. Based on this observation, the bimane system was utilized as a fluorophore within proteolytic enzyme substrates. Bimane peptides containing tryptophan (1a-1f) were prepared and shown to be potent fluorogenic substrates for the assay of chymotrypsin and aminopeptidase.

Original languageEnglish
Pages (from-to)298-306
Number of pages9
JournalBioorganic Chemistry
Volume16
Issue number3
DOIs
StatePublished - Sep 1988

Fingerprint

Dive into the research topics of 'Organic fluorescent reagents. XIV. Novel fluorogenic substrates for microdetermination of chymotrypsin and aminopeptidase: Bimane fluorescence appears after hydrolysis'. Together they form a unique fingerprint.

Cite this