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|Title:||Human L-ficolin: Plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain|
|Citation:||Le, 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|
|Abstract:||Ficolins 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.|
|Source Title:||FEBS Letters|
|Appears in Collections:||Staff Publications|
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