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*
Department of Medical Microbiology and Immunology, University of Aarhus, Aarhus, Denmark;
Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom; and
Immunology and Microbiology, Institute of Medical Biology, University of Southern Denmark, Odense, Denmark
Mannan-binding lectin (MBL) is a serum protein that
activates the complement system after binding to glycoconjugates found
on the surface of microorganisms. By molecular cloning two forms of MBL
have been identified in the mouse (mMBL-A and mMBL-C), but only mMBL-A
has been purified and characterized at the protein level. MBL-C has
been termed the liver form of MBL. The present report describes the
purification and characterization of mMBL-A and mMBL-C from serum. The
two forms of mMBL could be separated both by ion-exchange and
carbohydrate-affinity chromatography. The initial identification by
immunochemical technique was confirmed by N-terminal amino-acid
sequencing. Both proteins give bands corresponding to polypeptide
chains of 28 kDa on SDS-PAGE in the reduced state, but mMBL-A migrated
more rapidly than mMBL-C in acid/urea-PAGE, in accordance with the
calculated pIs. Both forms mediated activation of complement component
C4 in mannan-coated microtiter wells. MBL-A showed a higher affinity
for D-glucose and 
-methyl-D-glucose then did
MBL-C. Serum concentrations of mMBL-A in laboratory strains and wild
mice were found to vary from 5 to 80 µg/ml, with wild mice tending to
show higher levels than laboratory strains.
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