Isolation and characterization of a mannan-binding protein from human serum.
A serum lectin specific for mannose and N-acetylglucosamine residues was isolated from human serum to near homogeneity mainly by affinity chromatography on a column of Sepharose 4B-mannan. The lectin, called mannan-binding protein, was a glycine-rich protein with an apparent molecular size of approximately 600,000 daltons, and had a subunit structure consisting of a single component with an apparent molecular weight of 31,000. Binding of the isolated lectin to 125I-labeled mannan was dependent upon the presence of Ca2+, proportional to the protein added, and a reversible and saturable process. Scatchard plot analysis of binding data indicated the presence of a binding site with a dissociation constant of 2.3 X 10(-9) M and a maximum capacity of 4.3 pmol of 125I-labeled mannan per microgram of protein (2.6 mol of mannan per mol of the protein). The mannan-binding protein, is different from C-reactive protein (CRP) and amyloid P-component (SAP), both of which are serum components known to bind polysaccharides in the presence of Ca2+. A distinct binding activity toward mannan which did not require Ca2+ was attributed to immunoglobulins (IgG).
D000596:Amino Acids / Q000032:analysis; D002118:Calcium / Q000494:pharmacology; D002352:Carrier Proteins / Q000097:blood* / Q000302:isolation & purification; D037222:Collectins; D006801:Humans; D007700:Kinetics; D008351:Mannans / Q000097:blood*; D008970:Molecular Weight; D012794:Sialic Acids / Q000032:analysis; D013329:Structure-Activity Relationship
D000596:Amino Acids; D002352:Carrier Proteins; D037222:Collectins; D008351:Mannans; D012794:Sialic Acids; D002118:Calcium