Please use this identifier to cite or link to this item: https://doi.org/10.1016/0167-4838(93)90076-4
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dc.titleTwo forms of Factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation
dc.contributor.authorDing, J.L.
dc.contributor.authorNavas, III M.A.A.
dc.contributor.authorHo, B.
dc.date.accessioned2012-03-28T06:06:04Z
dc.date.available2012-03-28T06:06:04Z
dc.date.issued1993
dc.identifier.citationDing, 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
dc.identifier.issn01674838
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/31479
dc.description.abstractThe 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/0167-4838(93)90076-4
dc.sourceScopus
dc.subjectamoebocyte
dc.subjectC. rotundicauda
dc.subjectFactor C
dc.subjectprotein characterization
dc.subjectprotein purification
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.contributor.departmentZOOLOGY
dc.description.doi10.1016/0167-4838(93)90076-4
dc.description.sourcetitleBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
dc.description.volume1202
dc.description.issue1
dc.description.page149-156
dc.description.codenBBAED
dc.identifier.isiutA1993LY16100022
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