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  • Title: Isolation and characterization of two distinct mannan-binding proteins from rat serum.
    Author: Oka S, Ikeda K, Kawasaki T, Yamashina I.
    Journal: Arch Biochem Biophys; 1988 Jan; 260(1):257-66. PubMed ID: 3124748.
    Abstract:
    Two binding proteins, which are specific for mannose and N-acetylglucosamine, were isolated from rat serum to homogeneity. The minor component [serum mannan-binding protein I (S-MBP-I)] was indistinguishable from rat liver mannan-binding protein (L-MBP). S-MBP-I had a molecular mass of about 200 kDa and consisted of about six identical 32-kDa subunits; the molecule had a collagen-like structure, and its properties were identical to those of L-MBP. S-MBP-I was also indistinguishable from L-MBP in immunochemical reactivity. Furthermore, the sequence of 15 NH2-terminal amino acids of S-MBP-I was identical to that of L-MBP, the complete primary structure of which has been elucidated [Drickamer, K., Dordal, M. S., and Reynolds, L. (1986) J. Biol. Chem. 261, 6878-6887; Oka, S., Itoh, N., Kawasaki, T., and Yamashina, I. (1987) J. Biochem. 101, 135-144]. The major component (S-MBP-II) had a molecular mass of about 650 kDa and consisted of about 20 identical 31-kDa subunits; it was immunochemically distinct from L-MBP and S-MBP-I, although the molecule had a collagen-like structure similar to L-MBP and S-MBP-I. Metabolic studies using [3H]leucine showed that S-MBP-II is a typical plasma protein turning over with a half-life of 1.6 days. S-MBP-I was unusual in its late appearance and rapid turnover rate in plasma. These results, together with the fact that L-MBP decayed with biphasic curves, suggest that a part of L-MBP is leaked from liver into plasma in the form of S-MBP-I.
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