Advertisement

Purification and Characterization of Lectin from Lathyrus sativus

  • Vibha Malhotra Sawhney
  • I. M. Santha
  • Michael P. Timko
  • S. L. Mehta
Article

Abstract

Lectin has been isolated and purified from Lathyrus sativus using ammonium sulphate precipitation followed by affinity chromatography. The molecular weight as determined by HPLC was found to be 42kD. The lectin is a tetramer, consisting of two types of subunits of which the heavier subunit consists of 2 polypeptides of mol wt of about 21 kD and 16 kD while the smaller subunits consists of two polypeptides of about 5kD as revealed by SDS-PAGE. The most potent sugar inhibitor of the Lathyrus lectin was found to be α-methyl D-mannoside. The N-terminal amino acid sequence was similar to that of pea lectin sequence.

Key words

Lathyrus sativus lectin molecular characterization carbohydrate specificity amino acid sequence 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Chrispeels MJ & Raikhei NV, Plant Cell, 3 (1991)1.PubMedGoogle Scholar
  2. 2.
    Marban-Mendoza. N, Dicklow MB & Zuckerman BM, Funda Appl Nematoll, 15 (1992) 97.Google Scholar
  3. 3.
    Smith GB & Wollum AG, Can J Micro, 39 (1993) 245.CrossRefGoogle Scholar
  4. 4.
    Hilder UA, In Workshop on engineering plants against pests and patogens (G Bruening, F GarciaoiLmedo, Ponz F,Editors) 11–13 Jan. 1993 Madrid, Spain, p 68.Google Scholar
  5. 5.
    Roy PK, Singh B, Mehta SL, Barat GK, Gupta N, Kirti PB & Chopra VL, Ind J Exptl Biol, 29 (1991) 327.Google Scholar
  6. 6.
    Roy PK, Barat GK and Mehta SL, Plant Cell Tiss & Org Cult, 29 (1992) 135.CrossRefGoogle Scholar
  7. 7.
    Roy PK, All K, Gupta A, Barat GK & Mehta SL, J Plant Biochem Biotech, 2 (1993) 9.Google Scholar
  8. 8.
    Mehta SL, All K & Barna KS, J Plant Biochem Biotech, 3 (1994) 73.Google Scholar
  9. 9.
    Lowry OH, Rosenborough NJ, Farr AL & Randell RJ, J Biol Chem, 193 (1951) 265.PubMedGoogle Scholar
  10. 10.
    Laemmll UK, Nature, 227 (1970) 680.CrossRefGoogle Scholar
  11. 11.
    Pusztal A, Croy RRD, Grant G & Stewart JC. In Seed proteins (J Doussant, J Mosse & J Vaughan, Editors) New York, Academic Press (1983) p 53.Google Scholar
  12. 12.
    Van Damme JM, Goossens K, Smeets K, Van Leuven F, Verhaert P & Peumans WJ, PI Physiol, 107 (1995) 1147.CrossRefGoogle Scholar
  13. 13.
    Wang JL, Cunningham BA & Edelman GM, Proc Natl Acad Sci, USA, 68 (1971) 1130.PubMedCrossRefGoogle Scholar
  14. 14.
    Edmundson AB, Biochemistry, 10 (1971) 3554.PubMedCrossRefGoogle Scholar
  15. 15.
    Abe Y, Iwabuchi M & Ishii S, Biochem Biophys Res Commun, 46 (1971) 1271.CrossRefGoogle Scholar
  16. 16.
    Gupta BKD, Chatterjee-Ghose R & Sen A, Arch Biochem Blophys, 201 (1980) 137.CrossRefGoogle Scholar
  17. 17.
    Rejholcova M & Kocourek J, In Abstr 10th FEBs Meeting, Paris # 992 (1975).Google Scholar
  18. 18.
    Kolberg J & Sletten K,G. Biochem Biophys Acta, 704 (1982) 26.PubMedCrossRefGoogle Scholar
  19. 19.
    Higgins TJV, Chandler PM, Zurawski G, Button SC & Spencer D, J. Blochem, 258 (1983) 9544.Google Scholar

Copyright information

© Springer 1996

Authors and Affiliations

  • Vibha Malhotra Sawhney
    • 1
  • I. M. Santha
    • 1
  • Michael P. Timko
    • 1
  • S. L. Mehta
    • 1
  1. 1.Division of BiochemistryIndian Agricultural Research InstituteNew DelhiIndia

Personalised recommendations