The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Kinetical Properties of the Serum Mannan-Binding Protein from Rabbit.1 A Comparison with Those of the Liver Mannan-Binding Protein
Yasunori KOZUTSUMIToshisuke KAWASAKIIkuo YAMASHINA
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JOURNAL FREE ACCESS

1981 Volume 90 Issue 6 Pages 1799-1807

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Abstract

A serum lectin specific for mannose and N-acetylglucosamine residues (serum mannan-binding protein) was characterized as a glycine-rich protein of large molecular size. Binding of the lectin to 125I-labeled mannan was a reversible and saturable process with a dissociation constant of 2.3×10-9 M and a maximum capacity of 3.6 pmol of 125I-labeled mannan per pg of protein. α-Mannosidase, a lysosomal enzyme isolated from porcine kidney, bound to the lectin with high affinity (Kd=2.8×10-9 M). These kinetical parameters are compared with those of the liver mannan-binding protein in a discussion of the interrelationship of these two lectins.

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© The Japanese Biochemical Society
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