C R Babu

University of Delhi, Old Delhi, NCT, India

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Publications (62)121.32 Total impact

  • Amit Love, B D Banerjee, C R Babu
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    ABSTRACT: Assessment of oxidative stress levels and tissue concentrations of elements in plants growing wild on fly ash basins is critical for realistic hazard identification of fly ash disposal areas. Hitherto, levels of oxidative stress markers in plants growing wild on fly ash basins have not been adequately investigated. We report here concentrations of selected metal and metalloid elements and levels of oxidative stress markers in leaves of Cassia occidentalis growing wild on a fly ash basin (Badarpur Thermal Power Station site) and a reference site (Garhi Mandu Van site). Plants growing on the fly ash basin had significantly high foliar concentration of As, Ni, Pb and Se and low foliar concentration of Mn and Fe compared to the plants growing on the reference site. The plants inhabiting the fly ash basin showed signs of oxidative stress and had elevated levels of lipid peroxidation, electrolyte leakage from cells and low levels of chlorophyll a and total carotenoids compared to plants growing at the reference site. The levels of both protein thiols and nonprotein thiols were elevated in plants growing on the fly ash basin compared to plants growing on the reference site. However, no differences were observed in the levels of cysteine, reduced glutathione and oxidized glutathione in plants growing at both the sites. Our study suggests that: (1) fly ash triggers oxidative stress responses in plants growing wild on fly ash basin, and (2) elevated levels of protein thiols and nonprotein thiols may have a role in protecting the plants from environmental stress.
    Environmental Monitoring and Assessment 01/2013; DOI:10.1007/s10661-012-3046-6 · 1.68 Impact Factor
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    ABSTRACT: A. assamensis is a phytophagous Lepidoptera from Northeast India reared on host trees of Lauraceae family for its characteristic cocoon silk. Source of these cocoons are domesticated farm stocks that crash frequently and/or wild insect populations that provide new cultures. The need to reduce dependence on wild populations for cocoons necessitates assessment of genetic diversity in cultivated and wild populations. Molecular markers based on PCR of Inter-simple sequence repeats (ISSR) and simple sequence repeats (SSR) were used with four populations of wild insects and eleven populations of cultivated insects. Wild populations had high genetic diversity estimates (H i = 0.25; H S = 0.28; H E = 0.42) and at least one population contained private alleles. Both marker systems indicated that genetic variability within populations examined was significantly high. Among cultivated populations, insects of the Upper Assam region (H i = 0.19; H S = 0.18; H E = 0) were genetically distinct (F ST = 0.38 with both marker systems) from insects of Lower Assam (H i = 0.24; H S = 0.25; H E = 0.3). Sequencing of polymorphic amplicons suggested transposition as a mechanism for maintaining genomic diversity. Implications for conservation of native populations in the wild and preserving in-farm diversity are discussed.
    PLoS ONE 11/2012; 7(11):e49972. DOI:10.1371/journal.pone.0049972 · 3.53 Impact Factor
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    S. Babu, A. Love, C. R. Babu
    Ecological Restoration 11/2009; 27(4):467-477. DOI:10.3368/er.27.4.467
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    ABSTRACT: A novel serine protease inhibitor (AmPI) was purified from larval hemolymph of tasar silkworm, Antheraea mylitta by two-step process of trypsin-affinity and gel-filtration (FPLC) chromatography. AmPI was active against larval midgut and commercial bovine trypsin and chymotrypsin. The extent of purification was determined by SDS and Native PAGE. The protease inhibitor had an apparent molecular weight of approximately 14.5 kDa as determined by SDS-PAGE. Its activity was stable over a pH range of 4.5-9 and temperatures range of 4-65 degrees C. Molecular weight as determined by MALDITOF-MS was between 13241.63 and 13261.66 Da. MS profile of AmPI also suggests two isoforms of AmPI because of glycosylation by heptose (C(7)H(14)O(7)). This confirmed the result of Native PAGE showing two bands. N-terminal amino acid sequence of this protein did not show similarity to any known protease inhibitor. To study the functional implications of AmPI in insect, it was localized in insect body tissue of different larval instars by immunogold labeling technique using GAR-gold conjugate as secondary antibody. The pattern of localization suggests constitutive nature of AmPI, which may have role in insect's defense mechanism.
    Peptides 09/2009; 31(3):474-81. DOI:10.1016/j.peptides.2009.08.021 · 2.61 Impact Factor
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    ABSTRACT: Open dumping of fly ash in fly ash basins has significant adverse environmental impacts due to its elevated trace element content. In situ biomonitoring of genotoxicity is of practical value in realistic hazard identification of fly ash. Genotoxicity of openly disposed fly ash to natural plant populations inhabiting fly ash basins has not been investigated. DNA damage, and concentrations of As, Co, Cr, Cu and Ni in the leaves of natural populations of Cassia occidentalis growing at two contrasting sites-one having weathered fly ash (fly ash basin) and the other having soil (reference site) as plant growth substrates-were assessed. The foliar concentrations of As, Ni and Cr were two to eight fold higher in plants growing on fly ash as compared to the plants growing on soil, whereas foliar concentrations of Cu and Co were similar. We report, for the first time, based upon comet assay results, higher levels of DNA damage in leaf tissues of Cassia occidentalis growing wild on fly ash basin compared to C. occidentalis growing on soil. Correlation analysis between foliar DNA damage and foliar concentrations of trace elements suggests that DNA damage may perhaps be associated with foliar concentrations of As and Ni. Our observations suggest that (1) fly ash triggers genotoxic responses in plants growing naturally on fly ash basins; and (2) plant comet assay is useful for in situ biomonitoring of genotoxicity of fly ash.
    Ecotoxicology 06/2009; 18(7):791-801. DOI:10.1007/s10646-009-0322-5 · 2.50 Impact Factor
  • Amit Love, Suresh Babu, C. R. Babu
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    ABSTRACT: Extracts of roots of Rumex nepalensis, Berberis aristata, Arnebia benthamii, bark of Taxus wallichiana, Juglans regia and petals of Jacquinia ruscifolia were tested for their antifungal activity against twelve different fungal pathogens. Ethanolic extracts of R. nepalensis and J. ruscifolia extracts showed a broad spectrum of activity.
    Fitoterapia 08/2008; 79(7-8):589-91. DOI:10.1016/j.fitote.2008.06.004 · 2.22 Impact Factor
  • M. C. GOPINATHAN, C. R. BABU
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    ABSTRACT: Obligate subterranean cleistogamy, observed in a natural population of Vigna minima, is associated with the production of one or two negatively geotropic, leafy shoots and several positively geotropic, highly pigmented, leafless shoots. The latter branch profusely after penetrating the soil and produce much reduced, cleistogamous flowers. The undehisced anthers contain germinated pollen grains. The seeds developing from the cleistogamous flowers differ in size, weight and surface features from those produced by the chasmogamous flowers of other natural populations within the species.
    Botanical Journal of the Linnean Society 06/2008; 92(3):263 - 268. DOI:10.1111/j.1095-8339.1986.tb01431.x · 2.70 Impact Factor
  • Shruti Rai, K. K. Aggarwal, C. R. Babu
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    ABSTRACT: The roles of serine proteases involved in the digestion mechanism of the cutworm Spodoptera litura (Lepidoptera: Noctuidae) were examined (in vitro and in vivo) following feeding of plant protease inhibitors. A trypsin inhibitor from Archidendron ellipticum (AeTI) was purified by ammonium sulfate fractionation, ion-exchange chromatography and size-exclusion chromatography (HPLC) and its bioinsecticidal properties against S. litura were compared with Soybean Kunitz trypsin inhibitor (SBTI). AeTI inhibited the trypsin-like activities of the midgut proteases of fifth instar larvae of S. litura by over 70%. Dixon plot analysis revealed competitive inhibition of larval midgut trypsin and chymotrypsin by AeTI, with an inhibition constant (K(i)) of 3.5x10(-9) M and 1.5x10(-9) M, respectively. However, inhibitor kinetics using double reciprocal plots for both trypsin and chymotrypsin inhibitions demonstrated a mixed inhibition pattern. Feeding experiments conducted on different (neonate to ultimate) instars suggested a dose-dependent decrease for both the larval body weight as well as % survival of larva fed on diet containing 50, 100 and 150 microM AeTI. Influence of AeTI on the larval gut physiology indicated a 7-fold decrease of trypsin-like protease activity and a 5-fold increase of chymotrypsin-like protease activity, after being fed with a diet supplemented with 150 microM AeTI. This study suggests that although the early (1st to 3rd) larval instars of S. litura are susceptible to the trypsin inhibitory action of AeTI, the later instars may facilitate the development of new serine proteases, insensitive to the inhibitor.
    Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology 06/2007; 145(4):669-77. DOI:10.1016/j.cbpc.2007.03.003 · 2.83 Impact Factor
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    ABSTRACT: Evolution of proteinase inhibitor diversity in leguminous plants of tropical rainforests is under immense pressure from the regular upregulation of proteolytic machinery of their pests. The present study illustrates the isolation and bioinsecticidal potency of a serine proteinase inhibitor from the seeds of Caesalpinia bonduc (CbTI), inhabiting Great Nicobar Island, India. Following initial fractionation by ammonium sulfate precipitation, CbTI was purified to homogeneity by ion exchange, gel filtration and trypsin affinity chromatography. SDS-PAGE of gel filtrated CbTI showed a couple of proteins CbTI-1 ( approximately 16kDa) and CbTI-2 (20kDa) under non-reducing conditions, which subsequent to trypsin affinity chromatography yielded only CbTI-2. Both Native PAGE as well as iso-electric focusing showed 2 iso-inhibitors of CbTI-2 (pI values of 5.35 and 4.6). CbTI exhibited tolerance to extremes of temperatures (0-60 degrees C) and pH (1-12). A 1:1 stoichiometric ratio was noted during CbTI-2-trypsin complex formation, which was absent on binding with chymotrypsin. Further, SDS-PAGE analysis also showed that CbTI-1 has affinity only towards chymotrypsin, whereas both trypsin and chymotrypsin formed complexes with CbTI-2. Dixon plot analysis of CbTI-2 yielded inhibition constants (K(i)) of 2.75 x 10(-10)M and 0.95 x 10(-10)M against trypsin and chymotrypsin activity respectively. Preliminary investigations on the toxicological nature of CbTI revealed it to be a promising bioinsecticidal candidate.
    Plant Physiology and Biochemistry 03/2007; 45(3-4):169-77. DOI:10.1016/j.plaphy.2007.02.003 · 2.35 Impact Factor
  • A Bhattacharyya, C R Babu
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    ABSTRACT: A Kunitz proteinase inhibitor from Archidendron ellipticum seeds (AeTI) was purified and complexed with bovine trypsin and chymotrypsin. The stoichiometric stability of AeTI with its interacting proteinases was then investigated using spectrophotometric, size exclusion chromatography (HPLC system), Western blotting and circular dichroism (CD) studies. All the methods were remarkably similar in revealing the preference of trypsin over chymotrypsin by AeTI for complex formation. Both Western blotting as well as spectrophotometry based assays for competition experiments indicated that trypsin displaces chymotrypsin from a previously formed AeTI-chymotrypsin complex. Chemical modification of lysine and arginine by TNBS and CHD treatments, respectively, suggested a lysine as the active site residue and also indicated the presence of a single protease-binding site for AeTI. CD of native AeTI showed a sharp minimum at 200 nm and deconvolution of the CD spectra revealed it to be an unordered protein possessing high beta-sheet content. Complex formation of AeTI with trypsin induces a fractional switchover of its unordered structure towards the beta-sheet fraction but lacked any such conversion in the presence of chymotrypsin. Prolonged exposure of excess trypsin generates conformational modifications both in the secondary and the tertiary structures.
    Plant Physiology and Biochemistry 11/2006; 44(11-12):637-44. DOI:10.1016/j.plaphy.2006.10.008 · 2.35 Impact Factor
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    ABSTRACT: Mangroves form an important ecosystem of Great Nicobar, a continental island in the Bay of Bengal with luxuriant tropical rainforests. The rhizosphere of the mangrove plants of Great Nicobar was investigated for the presence of arbuscular mycorrhizal fungus (AMF) and phosphate solubilising bacteria (PSB). The soils of the Great Nicobar mangroves were silt–clays and were poor in phosphate content. Five species of AMF belonging to the genus Glomus were isolated. The %AMF colonization in the mangrove plants was between 0 and 17%, and the presence of AMF in the aerenchymatous cortex suggests that the mangrove plants may be aiding in AMF survival by providing oxygen. Two strains of phosphate solubilising Pseudomonas aeruginosa were found in the mangrove soils of Great Nicobar. Phosphate solubilisation by the two isolated strains was almost 70% under in vitro conditions. PSB may play a role in the mangrove ecosystems of Great Nicobar by mobilising insoluble phosphate. The plant roots could pick up the released phosphate directly or with the aid of AMF hyphae.
    Biology and Fertility of Soils 01/2006; 42(4):358-361. DOI:10.1007/s00374-005-0035-8 · 3.40 Impact Factor
  • A. Bhattacharyya, C.R. Babu
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    ABSTRACT: A Kunitz proteinase inhibitor from Archidendron ellipticum seeds (AeTI) was purified and complexed with bovine trypsin and chymotrypsin. The stoichiometric stability of AeTI with its interacting proteinases was then investigated using spectrophotometric, size exclusion chromatography (HPLC system), Western blotting and circular dichroism (CD) studies. All the methods were remarkably similar in revealing the preference of trypsin over chymotrypsin by AeTI for complex formation. Both Western blotting as well as spectrophotometry based assays for competition experiments indicated that trypsin displaces chymotrypsin from a previously formed AeTI–chymotrypsin complex. Chemical modification of lysine and arginine by TNBS and CHD treatments, respectively, suggested a lysine as the active site residue and also indicated the presence of a single protease-binding site for AeTI. CD of native AeTI showed a sharp minimum at 200 nm and deconvolution of the CD spectra revealed it to be an unordered protein possessing high β-sheet content. Complex formation of AeTI with trypsin induces a fractional switchover of its unordered structure towards the β-sheet fraction but lacked any such conversion in the presence of chymotrypsin. Prolonged exposure of excess trypsin generates conformational modifications both in the secondary and the tertiary structures.
    Plant Physiology and Biochemistry 01/2006; 44(11-12-44 (11-12)):637-644. · 2.35 Impact Factor
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    ABSTRACT: Mistletoe ribosome inactivating proteins (RIPs) are excellent immunomodulators obtained from a hemi-parasitic plant Viscum album L. In the present study, we have characterized and cloned a 65 kDa heterodimeric RIP from Himalayan V. album. Himalayan mistletoe ribosome inactivating protein (HmRIP) possessed unique sugar affinity for l-Rhamnose, Meso-inositol and l-Arabinose besides Galactose and N-acetyl-Galactosamine. The lectin activity was stable to a broad range of temperature (4–65 °C) and pH (2.5–12.5). cDNA cloning showed that HmRIP is 500 amino acids long and shortest among mistletoe RIPs. Amino acid sequence analyses revealed important differences at the functionally significant sites. In the lectin subunit, two critical residues forming base of the 2γ sugar-binding cleft were deleted. Such differences lead to a different conformation of sugar-binding cleft giving rise to unique sugar-binding properties of HmRIP. Toxin subunit also showed a sizeable deletion of four residue segment in the antigenic epitope (83–103) determining its antigenecity. Due to striking differences at the functional sites associated with medicinal properties, HmRIP is a novel type II RIP. In the phylogenetic tree based on amino acid sequence of type II RIPs from six dicot families, mistletoe RIPs branched out from the RIPs of all other taxa and formed a distinct and distant group supporting independent evolution of Viscaceae among the angiosperms.
    Plant Science 03/2005; DOI:10.1016/j.plantsci.2004.09.024 · 4.11 Impact Factor
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    ABSTRACT: Exposure of healthy wheat seeds (Triticum aestivum var Sonalika) to mild dose of cadmium (Cd(2+)) given as 50 microM CdCl(2) for 48 h and then washed off Cd(2+) offered resistance to the subsequent infection by Fusarium oxysporum inoculum. Seven days old seedlings having two primary leaves were aseptically inoculated with fungus, F. oxysporum (1 x 10(6)) spores. The seedlings pre-exposed to low level of Cd(2+) survived the Fusarium infection, while plantlets without Cd(2+) stress wilted and then perished due to Fusarium infection. The stress associated proteins induced by Cd(2+) (50 microM), F. oxysporum and by the co-stress (50 microM Cd(2+) and then with F. oxysporum) treatments were observed to be of same molecular weight (51 kDa). Antibody was raised against the purified Cd(2+)-stress associated protein (CSAP). Immuno-gold labeling of wheat seedling root tissue showed the presence of this CSAP in Cd(2+) pre-exposed and in co-stressed tissues and to be located predominantly on the inner linings of the cell membranes. We also observed that the anti-CSAP-antibody also labeled the root tissue of only Fusarium inoculated seedlings and the gold labeling was intensely located on the membrane. This cross-reaction of anti-CSAP suggests that Fusarium-induced stress protein (FISP) possibly has close homology to CSAP. We thus show for the first time the over expression of a high molecular mass protein by mild dose of Cd(2+) pre-exposure to wheat seeds which subsequently provided protection against Fusarium infection. This mode of resistance developed by an abiotic stress-causing agent against pathogen infection is novel.
    Plant Physiology and Biochemistry 01/2005; 42(10):781-7. DOI:10.1016/j.plaphy.2004.09.005 · 2.35 Impact Factor
  • Ram Singh, Geetanjali, C.R. Babu
    Chemistry & Biodiversity 01/2005; 2(4):429-446. · 1.80 Impact Factor
  • T Dam, C R Babu
    Journal of Medical Microbiology 10/2003; 52(Pt 9):843. DOI:10.1099/jmm.0.05144-0 · 2.27 Impact Factor
  • Acta Crystallographica Section A Foundations of Crystallography 08/2002; 58. DOI:10.1107/S0108767302096502 · 2.07 Impact Factor

Publication Stats

393 Citations
121.32 Total Impact Points

Institutions

  • 1979–2013
    • University of Delhi
      • • Department of Environmental Studies
      • • Centre of Environmental Management of Degraded Ecosystems
      • • Department of Botany (Faculty of Science)
      • • CSIR Centre for Biochemicals
      Old Delhi, NCT, India
  • 1980
    • Vallabhbhai Patel Chest Institute
      Old Delhi, NCT, India