Purification and characterization of a Ca 2+-dependent novel lectin from Nymphaea nouchali tuber with antiproliferative activities

Syed Rashel Kabir, Md Abu Zubair, Md Nurujjaman, Md Azizul Haque, Imtiaj Hasan, Md Farhadul Islam, Md Tanvir Hossain, Md Anowar Hossain, Md Abdur Rakib, Mohammad Taufiq Alam, Ranajit Kumar Shaha, Md Tofazzal Hossain, Yoshinobu Kimura, Nurul Absar

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

A lectin (termed NNTL) was purified from the extracts of Nymphaea nouchali tuber followed by anion-exchange chromatography on DEAE-cellulose, hydrophobic chromatography on HiTrap Phenyl HP and by repeated anion-exchange chromatography on HiTrap Q FF column. The molecular mass of the purified lectin was 27.0 ± 1.0 kDa, as estimated by SDS/PAGE both in the presence and in the absence of 2-mercaptoethanol. NNTL was an o-nitrophenyl β-D- galactopyranoside sugar-specific lectin that agglutinated rat, chicken and different groups of human blood cells and exhibited high agglutination activity over the pH range 5-9 and temperatures of 30-60°C. The N-terminal sequence of NNTL did not show sequence similarity with any other lectin and the amino acid analysis revealed that NNTL was rich in leucine, methionine and glycine residues. NNTL was a glycoprotein containing 8% neutral sugar and showed toxicity against brine shrimp nauplii with an LC 50 value of 120 ± 29 μg/ml and exerted strong agglutination activity against four pathogenic bacteria (Bacillus subtilis, Sarcina lutea, Shigella Shiga and Shigella sonnei). In addition, antiproliferative activity of this lectin against EAC (Ehrlich ascites carcinoma) cells showed 56% and 76% inhibition in vivo in mice at 1.5 and 3 mg·kg -1·day -1 respectively. NNTL was a divalent ion-dependent glycoprotein, which lost its activity markedly in the presence of denaturants. Furthermore, measurement of fluorescence spectra in the presence and absence of urea and CaCl 2 indicated the requirement of Ca 2+ for the stability of NNTL.

Original languageEnglish
Pages (from-to)465-475
Number of pages11
JournalBioscience Reports
Volume31
Issue number6
DOIs
Publication statusPublished - Dec 1 2011

Keywords

  • Antiproliferative activity
  • Bacterial agglutination
  • Fluorescence spectroscopy
  • Hydrophobic chromatography
  • Ion-exchange chromatography
  • Toxicity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Purification and characterization of a Ca <sup>2+</sup>-dependent novel lectin from Nymphaea nouchali tuber with antiproliferative activities'. Together they form a unique fingerprint.

  • Cite this

    Kabir, S. R., Zubair, M. A., Nurujjaman, M., Haque, M. A., Hasan, I., Islam, M. F., Hossain, M. T., Hossain, M. A., Rakib, M. A., Alam, M. T., Shaha, R. K., Hossain, M. T., Kimura, Y., & Absar, N. (2011). Purification and characterization of a Ca 2+-dependent novel lectin from Nymphaea nouchali tuber with antiproliferative activities. Bioscience Reports, 31(6), 465-475. https://doi.org/10.1042/BSR20100126