Literature DB >> 1550571

Human mannose-binding protein is identical to a component of Ra-reactive factor.

M Matsushita1, A Takahashi, H Hatsuse, M Kawakami, T Fujita.   

Abstract

Human Ra-reactive factor (RaRF) and mannose-binding protein (MBP) were isolated from sera by utilizing their affinity to Ra chemotype Salmonella typhimurium and yeast mannan, respectively. A predominant polypeptide of human RaRF with an Mr of 32 kDa (P32) has the same mobility as human MBP on SDS-PAGE gels. A monoclonal antibody against P32 of human RaRF, 3E7, was found to react not only with P32 but also with human MBP, as assessed by immunoblotting. In addition, 3E7 blocked the complement-activating capacity of human MBP. The NH2-terminal amino acid sequence of P32 of human RaRF was determined and found to coincide with that of human MBP. Based on these results, it is clear that human MBP is identical to a component of RaRF.

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Year:  1992        PMID： 1550571     DOI： 10.1016/0006-291x(92)90531-o

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  13 in total

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7.  Binding of mannose-binding protein to Klebsiella O3 lipopolysaccharide possessing the mannose homopolysaccharide as the O-specific polysaccharide and its relation to complement activation.

Authors:  G Z Jiang; T Sugiyama; Y Kato; N Koide; T Yokochi
Journal:  Infect Immun       Date:  1995-07       Impact factor: 3.441

8.  Human serum mannose-binding lectin (MBL)-associated serine protease-1 (MASP-1): determination of levels in body fluids and identification of two forms in serum.

Authors:  I Terai; K Kobayashi; M Matsushita; T Fujita
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9.  Mannose binding protein is involved in first-line host defence: evidence from transgenic mice.

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Journal:  Immunology       Date:  1995-05       Impact factor: 7.397

10.  Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease.

Authors:  M Matsushita; T Fujita
Journal:  J Exp Med       Date:  1992-12-01       Impact factor: 14.307
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