A Sensitive Substrate for the Clotting Enzyme in Horseshoe Crab Hemocytes1
- 1 May 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 81 (5) , 1567-1569
- https://doi.org/10.1093/oxfordjournals.jbchem.a131612
Abstract
An endotoxin-activated hemocyte lysate from horseshoe crab (Tachypleus and Limulus) was found to hydrolyze specifically BZ-Ile-Glu-Gly-Arg-p-nitroanilide, which was recently introduced as the substrate for assay of the blood coagulation factor, Factor Xa. Further, this amidase activity increased by increasing the concentration of bacterial endotoxin (Salmonella minnesota R595) added to the lysate. Thus, the measurement of the amidase activity in the hemocyte lysate can be very useful to detect and determine the endotoxin.This publication has 2 references indexed in Scilit:
- A Clottable Protein (Coagulogen) of Horseshoe Crab Hemocytes. Structural Change of Its Polypeptide Chain during Gel Formation1The Journal of Biochemistry, 1976
- Gram-Negative Sepsis: Detection of Endotoxemia with the Limulus TestAnnals of Internal Medicine, 1972