FEBS Letters | |
Human l‐ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen‐like (FBG) domain | |
Le, Y2  Kon, O.L2  Lu, J2  Lee, S.H1  | |
[1] Department of Pathology, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260, Singapore;National University Medical Institute, Blk MD11, #02-01 Clinical Research Centre, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260, Singapore | |
关键词: Ficolin; Fibrinogen-like domain; Collagen-like; Lectin; Collectin; C1q; FBG; fibrinogen β/γ C-terminal; GlcNAc; N-acetyl-d-glucosamine; GalNAc; N-acetyl-d-galactosamine; CRD; carbohydrate recognition domain; | |
DOI : 10.1016/S0014-5793(98)00267-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 showed that adult plasma contains approximately three times more l-ficolin than that of newborn babies.
【 授权许可】
Unknown
【 预 览 】
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