Literature DB >> 427207

Hydrophobicity of lectins. I. The hydrophobic character of concanavalin A.

J L Ochoa, T Kristiansen, S Påhlman.   

Abstract

The hydrophobicity of Concanavalin A has been estimated by its tendency to adsorb to hydrophobic adsorbents. Experiments varying temperature, salt concentration and hydrophobicity of the absorbent were consistent with accepted criteria of hydrophobic interaction between biomolecules and hydrophobic ligands. The biological significance of the hydrophobic character of Concanavalin A is also discussed.

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Year:  1979        PMID: 427207     DOI: 10.1016/0005-2795(79)90011-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Binding studies of a sialic acid-specific lectin from the horseshoe crab Carcinoscorpius rotunda cauda with various sialoglycoproteins.

Authors:  S Mohan; D Thambi Dorai; S Srimal; B K Bachhawat
Journal:  Biochem J       Date:  1982-04-01       Impact factor: 3.857

2.  Highly purified particulate guanylate cyclase from rat lung: characterization and comparison with soluble guanylate cyclase.

Authors:  S A Waldman; J A Lewicki; L Y Chang; F Murad
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396

3.  Differentiated microdomains on the luminal surface of capillary endothelium: distribution of lectin receptors.

Authors:  M Simionescu; N Simionescu; G E Palade
Journal:  J Cell Biol       Date:  1982-08       Impact factor: 10.539

  3 in total

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