http://nopr.niscair.res.in/handle/123456789/3232 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/3268 Title: Effect of endosulfan on growth, ⍺ amylase activity and plasmids amplification in Bacillus subtilis <br/> <br/>Authors: Tolan, Veysel; Ensari, Yavuz <br/> <br/>Abstract: Endosulfan, a chlorinated hydrocarbon insecticide of cyclodiene subgroup acts as a contact poison in a wide variety of organisms. In the present study, the effect of endosulfan on the growth, α amylase activity and plasmid amplification was investigated in Bacillus subtilis system. The bacteria were grown in medium, incubated with different concentrations (32, 48, 64 and 80 μg/mL) of endosulfan. The bacterial growth was gradually seen after 1st day at up to 48 μg/L endosulfan. The 48 μg/L endosulfan inhibited approximately 50% of the bacterial growth. No growth was observed at and after 64 μg/L endosulfan, for all days (1-5). Also, no ⍺ amylase activity was found in the supernatant of the culture medium containing 64 and 80 μg/L endosulfan, whereas slight activity was observed with 32 and 48 μg/L endosulfan concentration. The amount of plasmid increased up to 50% in the presence of 32 μg/L endosulfan. Endosulfan had no effect on the ⍺ amylase activity in vitro. <br/> <br/>Page(s): 123-126 http://nopr.niscair.res.in/handle/123456789/3267 Title: Rapid regulatory effect of tri-iodothyronine (T₃) on antioxidant enzyme activities in a fish Anabas testudineus (Bloch): Short-term in vivo and in vitro study <br/> <br/>Authors: Sreejith, P; Oommen, O V <br/> <br/>Abstract: The short-term action of thyroid hormone tri-iodothyronine (T₃) was studied in vivo and in vitro on antioxidant enzyme activities in a teleost Anabas testudineus (Bloch). T₃ injection in vivo (200 ng) in normal fish decreased the lipid peroxidation products and increased superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) activities after 30 min. T₃ in vitro (10⁻⁶ M) increased the antioxidant activities of catalase, glutathione reductase (GR), GPx and glutathione level after 15/30 min, except SOD, substantiating in vivo effects in normal fish. The results suggest a rapid regulatory effect of thyroid hormone in vivo and in vitro, in the removal of reactive oxygen species in A. testudineus. <br/> <br/>Page(s): 119-122 http://nopr.niscair.res.in/handle/123456789/3266 Title: Ficus cunia agglutinin for recognition of bacteria <br/> <br/>Authors: Adhya, M; Singha, B; Chatterjee, B P <br/> <br/>Abstract: Interaction of bacteria with lectin using anti-lectin antibody by ELISA is an established method. In the present study, we have devised a simple ELISA using a biotinylated lectin and antibiotin-HRP. Ficus cunia agglutinin (FCA), which has shown the specificity towards / anomers of GlcNAc and other –NAc containing sugars like LacNAc and GlcNAc β(1-4/6)GlcNAc, was used as a model lectin for the study of interaction with immobilized microorganisms on ELISA plate. The bacterial cells of E. coli, Pseudomonas aeruginosa, Klebsiella pneumoniae, Bacillus subtilis and Staphylococcus aureus showed binding with FCA and the degree of binding was dependent on the bacterial surface antigen. This method is considered a simple technique to study the lectin-bacteria interaction. <br/> <br/>Page(s): 94-97 http://nopr.niscair.res.in/handle/123456789/3265 Title: Induction, purification and characterization of an antibacterial peptide scolopendrin I from the venom of centipede Scolopendra subspinipes mutilans <br/> <br/>Authors: Wenhua, Ren; Shuangquan, Zhang; Daxiang, Song; Kaiya, Zhou; Guang, Yang <br/> <br/>Abstract: The crude venom of the centipede Scolopendra subspinipes mutilans, injected with Escherichia coli K₁₂D₃₁ for 3-4 days showed broad-spectrum antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. It showed good antibacterial activity against E. coli K₁₂D₃₁ at different temperatures, pH, and ionic strengths. The crude venom was heated at 100°C for 30 min, centrifuged at 10,000 rpm for 30 min at 4°C and the supernatants were obtained, from which an antibacterial fraction having a molecular mass of 3000-5000 Da, was further separated by ultrafiltration. A homogeneous antibacterial peptide named scolopendrin I, having a molecular mass of 4,498 Da, was isolated using cation-exchange chromatography and two steps of reverse-phase high performance liquid chromatography (RP-HPLC). Scolopendrin I did not show any hemolytic and agglutination activities at the concentration below 30 μM. <br/> <br/>Page(s): 88-93