Purification and Characterization of Abrus precatorius Agglutinin

DOI HANDLE Open Access
  • Absar Nural
    Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University
  • Funatsu Gunki
    Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

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Abstract

Abrus pvecatorius agglutinin (APA) has been purified by a new purification procedure from the seeds of semen jequiriti produced in Bangladesh and Taiwan. The method was accomplished by 33-50% saturation ammonium sulfate fraction from 1% acetic acid extract of the seeds of semen jequiriti using gel filtration on Sephadex G-75 followed by DEAE-cellulose column chromatography. The molecular weight was estimated to be 126,000 and 122,000 by gel filtration on Sephadex G-150 for Bangladesh-APA and Taiwan-APA, respectively. Both the APA were found to be consist of two types of polypeptide chains of nearly same size (30,000 to 34,000), which possess valine and proline as N-terminal amino acid. Furthermore, one of the constituent polypeptide chains of APA showed microheterogeneity, suggesting that APA is a mixture of isolectins.

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Details 詳細情報について

  • CRID
    1390853649614452736
  • NII Article ID
    110000017524
  • NII Book ID
    AA00247166
  • DOI
    10.5109/23798
  • HANDLE
    2324/23798
  • ISSN
    00236152
  • Text Lang
    en
  • Data Source
    • JaLC
    • IRDB
    • Crossref
    • CiNii Articles

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