alexa Chromogenic substrates for horseshoe crab clotting enzyme. Its application for the assay of bacterial endotoxins.
Chemical Engineering

Chemical Engineering

Journal of Analytical & Bioanalytical Techniques

Author(s): Iwanaga S, Morita T, Harada T, Nakamura S, Niwa M,

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Abstract An endotoxin-activated hemocyte lysate from the horseshoe crab (Tachypleus and Limulus) was found to hydrolyze Bz-Ile-Glu-(gamma-OR)-Gly-Arg-p-nitroanilide (PNA), Bz-Val-Gly-Arg-PNA, Boc-Val-Leu-Gly-Arg-PNA, and Boc-Leu-Gly-Arg-PNA, all of which have the COOH-terminal Gly-Arg sequence. This amidase activity was due to a clottting enzyme contained in the lysate. Furthermore, the amidase activity increased by increasing the concentration of bacterial endotoxin (E. coli, 0111-B4) added to the lysate. Therefore, the measurement of the endotoxin-induced amidase activity made it possible to determine the concentration of the endotoxin.
This article was published in Haemostasis and referenced in Journal of Analytical & Bioanalytical Techniques

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