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Human l ‐ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen‐like (FBG) domain
Author(s) -
Le Y,
Lee S.H,
Kon O.L,
Lu J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00267-1
Subject(s) - ficolin , lectin , chemistry , fibrinogen , biochemistry , cord blood , collagenase , glycoprotein , galactosamine , glucosamine , biology , enzyme , immunology , mannan binding lectin
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.