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Published on: October 6, 2022
Detection of hydrolytic activity of trypsin with a fluorescence-chymotryptic peptide on a TLC plate
Tetsuya Uchikoba1, Shigeko Fukumoto, Takao Itakura
1Kagoshima University Musium, Kagoshima, Japan. uchik@sci.kagshima-u.ac.jp
Abstract:
To find a new trypsin-like enzyme, a simple assay method of the hydrolysis activity for trypsin has been found. We used 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) in the peptide labeling as a substrate for the trypsin-like peptidase in this study. The peptidase activity of trypsin was detected by using an AQC-chymotryptic peptide (AHP1) obtained from bovine hemoglobin. This showed that the substrate specificity of trypsin-like peptidase was distinguishable from that of the others by this procedure, and the method was used extensively in cases of various trypsin inhibitors with no significant interference from the concomitant.
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