Isolation and characterization of a mannan-binding protein from human serum

J Biochem. 1983 Sep;94(3):937-47. doi: 10.1093/oxfordjournals.jbchem.a134437.

Abstract

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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Calcium / pharmacology
  • Carrier Proteins / blood*
  • Carrier Proteins / isolation & purification
  • Collectins
  • Humans
  • Kinetics
  • Mannans / blood*
  • Molecular Weight
  • Sialic Acids / analysis
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Carrier Proteins
  • Collectins
  • Mannans
  • Sialic Acids
  • Calcium