Please use this identifier to cite or link to this item: https://doi.org/10.1016/0167-4838(93)90076-4
Title: Two forms of Factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation
Authors: Ding, J.L. 
Navas, III M.A.A.
Ho, B. 
Keywords: amoebocyte
C. rotundicauda
Factor C
protein characterization
protein purification
Issue Date: 1993
Source: Ding, J.L., Navas, III M.A.A., Ho, B. (1993). Two forms of Factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1202 (1) : 149-156. ScholarBank@NUS Repository. https://doi.org/10.1016/0167-4838(93)90076-4
Abstract: The two apparent forms of the endotoxin-sensitive Factor C which were found to exist in the amoebocytes of horseshoe crabs have been separately purified to homogeneity from the lysate of the South-East Asian species, Carcinoscorpius rotundicauda. Both forms are serine proteinase zymogens having an apparent molecular mass of 132 kDa. By reducing SDS-PAGE, one was shown to consist of a single polypeptide while the other has a heavy chain (80 kDa) and a light chain (52 kDa) bridged by disulfide linkage(s). Both zymogen forms have endotoxin (lipopolysaccharide) receptors to which endotoxin binds to activate their catalytic sites. However, single-chain Factor C appears to have higher-affinity endotoxin-binding sites which are competitively but reversibly occupied by DMSO when the latter was added during its purification. Another salient difference between the two forms of Factor C is exhibited in their manner of activation by endotoxin. While double-chain Factor C appears similar to that of Tachypleus tridentatus, single-chain Factor C did not undergo any proteolytic cleavage upon activation. This conformational transition of zymogen activation suggests an alternative reversible pathway of endotoxin activation for the single-chain Factor C.
Source Title: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
URI: http://scholarbank.nus.edu.sg/handle/10635/31479
ISSN: 01674838
DOI: 10.1016/0167-4838(93)90076-4
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