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Purification and characterization of a lectin from Macrobrachium rosenbergh (Crustacea, Decapoda) hemolymph

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, ISSN: 0305-0491, Vol: 105, Issue: 3, Page: 617-623
1993
  • 54
    Citations
  • 0
    Usage
  • 9
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    54
    • Citation Indexes
      54
  • Captures
    9

Article Description

1.1. We have purified a 19 kDa lectin from the freshwater prawn Macrobrachium rosenbergii by single-step affinity chromatography on a rat stroma column.2.2. The lectin is a glycoprotein composed of two monomeric subunits of 9.6 kDa bound by a disulfide bridge; 7% of its contents are carbohydrates.3.3. It has an S20, w value of 1.4, a pI of 5.4–6.1, and is rich in glycine, serine, glutamic and aspartic acid residues.4.4. It requires divalent cations to function.5.5. It recognizes sialic acid.6.6. The hemagglutinating and hapten inhibition assays strongly suggest that it is 9-O-acetylsialic acid residue-specific.

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