Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(98)00267-1
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dc.titleHuman L-ficolin: Plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain
dc.contributor.authorLe, Y.
dc.contributor.authorLee, S.H.
dc.contributor.authorKon, O.L.
dc.contributor.authorLu, J.
dc.date.accessioned2014-05-20T02:29:34Z
dc.date.available2014-05-20T02:29:34Z
dc.date.issued1998-03-27
dc.identifier.citationLe, Y., Lee, S.H., Kon, O.L., Lu, J. (1998-03-27). Human L-ficolin: Plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain. FEBS Letters 425 (2) : 367-370. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(98)00267-1
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/53442
dc.description.abstractFicolins are characterised by the presence of collagen-like and fibrinogen-like (FBG) sequences. Human L-ficolin is synthesised in the liver and secreted into blood circulation. In previous studies, it was shown to bind to N-acetyl-D-glucosamine (GlcNAc). In the present study, its detailed sugar specificity and binding site have been investigated. It was found to bind to GlcNAc and GalNAc (N-acetyl-D-galactosamine) while showing no significant affinity for the precursor sugars. The structure in these molecules which is recognised by L-ficolin has been deduced to include an amide (-CO-NH-) or similar group. L-Ficolin was digested with collagenase and the collagenase resistant FBG domain was shown to bind to GlcNAc. Its levels in adult and cord blood-derived human plasma were also determined and shelved that adult plasma contains approximately three times more L-ficolin than that of newborn babies.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0014-5793(98)00267-1
dc.sourceScopus
dc.subjectClq
dc.subjectCollagen-like
dc.subjectCollectin
dc.subjectFibrogen-like domain
dc.subjectFicolin
dc.subjectLectin
dc.typeArticle
dc.contributor.departmentNATIONAL UNIVERSITY MEDICAL INSTITUTES
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/S0014-5793(98)00267-1
dc.description.sourcetitleFEBS Letters
dc.description.volume425
dc.description.issue2
dc.description.page367-370
dc.description.codenFEBLA
dc.identifier.isiut000073061400038
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