A clottable protein (coagulogen) of horseshoe crab hemocytes. Structural change of its polypeptide chain during gel formation.
A clottable protein (coagulogen) isolated from a hemocyte lysate of the Japanese horseshoe crab (Tachypleus tridentatus) was incubated with an endotoxin-activated clotting enzyme(s) partially purified from the same lysate, and its structural change during gel formation was examined. The results indicated that the enzymatic formation of gel involved limited proteolysis of the Arg-Gly and Arg-Thr linkages located in the N-terminal portion of the coagulogen, liberating peptide C.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001427:Bacterial Toxins / Q000494:pharmacology; D001777:Blood Coagulation; D001798:Blood Proteins / Q000378:metabolism*; D005782:Gels; D006737:Horseshoe Crabs / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012475:Salmonella
D000596:Amino Acids; D001427:Bacterial Toxins; D001798:Blood Proteins; D005782:Gels; D010446:Peptide Fragments; C013445:coagulogen