Document Detail

Studies on Limulus amoebocyte lysate II. Purification of the coagulogen and the mechanism of clotting.
MedLine Citation:
PMID:  873916     Owner:  NLM     Status:  MEDLINE    
A coagulogen in Limulus lysate has been purified to apparent homogeneity as judged by sodium dodecyl sulfate-gel electrophoresis. The purified coagulogen identified by its ability to clot with either trypsin or the purified Limulus clotting enzyme (Tai, J.Y., and Liu, T. Y. (1976) Fed. Proc. 35, 1486) has a molecular weight of 24,500. It consists of a single polypeptide chain of about 220 amino acids with glycine and serine as its NH2- and COOH-terminal residues; respectively. When acted upon by the Limulus clotting enzyme, the coagulogen releases a soluble C-peptide of about 45 amino acids and an insoluble coagulin of about 170 amino acids. The latter interacts in a noncovalent fashion to form the clot. Amino acid analyses together with the results of NH2- and COOH-terminal analyses suggest that the clot formation involves the cleavage of an--Arg--Lys--bond. Trypsin acts on the coagulogen to cause clotting by splitting the same peptide bond.
J Y Tai; R C Seid; R D Huhn; T Y Liu
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  252     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1977 Jul 
Date Detail:
Created Date:  1977-08-25     Completed Date:  1977-08-25     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4773-6     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Blood Coagulation
Blood Proteins / isolation & purification*,  metabolism
Electrophoresis, Polyacrylamide Gel
Endopeptidases / metabolism
Endotoxins / metabolism
Horseshoe Crabs
Peptide Fragments
Reg. No./Substance:
0/Amino Acids; 0/Blood Proteins; 0/Endotoxins; 0/Peptide Fragments; EC 3.4.-/Endopeptidases; EC

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