http://nopr.niscair.res.in/handle/123456789/2369 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/3132 Title: Book Review <br/> <br/>Authors: Mohanty, Prasanna <br/> <br/>Abstract: Advances in Photosynthesis and Respiration (AIPH) (Series Editor: Govindjee, University of Illinois, USA). Volume 26: “Biophysical Techniques in Photosynthesis II (Edited by Thijs J Aarsma and Jörg Matysik); Published by Springer, The Netherlands, 2008. ISBN: 976-1-4020-8249-8 (hardcover), 520 pages, & colour plates. <br/> <br/>Page(s): 354-355 http://nopr.niscair.res.in/handle/123456789/2378 Title: Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants <br/> <br/>Authors: Ghosh, Kallol K; Verma, Santosh Kumar <br/> <br/>Abstract: The kinetics of α-chymotrypsin (α-CT) catalyzed hydrolysis of 4-nitrophenyl acetate has been studied in aqueous solution of alkyldimethylethanolammonium bromide (cetyl, dodecyl, decyl) surfactants at concentrations below and above their critical micelle concentration. From Michaelis-Menten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of α-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate. <br/> <br/>Page(s): 350-353 http://nopr.niscair.res.in/handle/123456789/2377 Title: Enzymatic characteristics of quercetinases from some indigenous Aspergillus flavus strains <br/> <br/>Authors: Yadav, R S S; Yadav, K D S <br/> <br/>Abstract: Five indigenous Aspergillus flavus strains MTCC-2206, 1884, 1883, 1783 and 2456 were screened for the secretion of quercetinase. Fungal strains MTCC-2206, 1884, 1883, and 1783 were found to secrete the quercetinase in the range of 0.24-0.36 enzyme unit/mL of the culture medium, while MTCC-2456 secreted only 0.04 enzyme unit/mL. The enzymatic characteristics of quercetinase were determined. The Km values using quercetin as the substrate were 12.5 μM, 14.0 μM, 12.5 μM and 13.0 μM for the quercetinase produced by MTCC-2206, 1884, 1883 and 1783, respectively. The pH optima for the above enzymes were 6.5, 6.5, 6.0 and 6.0 and temperature optima were 45, 40, 45 and 50ºC, respectively. The partial purification from only one strain MTCC- 2206 was achieved (nearly 3-fold purification). <br/> <br/>Page(s): 345-349 http://nopr.niscair.res.in/handle/123456789/2376 Title: Suppressive effect of Strychnos nux-vomica on induction of ovalbumin-specific IgE antibody response in mice <br/> <br/>Authors: Duddukuri, Govinda Rao; Brahmam, A Naga; Rao, D N <br/> <br/>Abstract: Strychnos nux-vomica Linn. (SNV; Loganiaceae), a medicinal plant has been used as folk medicine for alleviating inflammation, joint pains and allergic symptoms. In the present study, we examined its possible immunomodulatory effect on induction of ovalbumin (OVA)-specific IgE antibody response in a murine model, as evaluated by passive cutaneous anaphylaxis (PCA). The OVA-specific IgE antibody response was significantly suppressed in BALB/c mice (H-2d), following intraperitoneal administration of aqueous stem extract of the plant along with OVA. Furthermore, the different doses of SNV extract were found to significantly suppress the induction of OVA-specific IgE antibody response. The anti-OVA IgE antibody response was suppressed in different haplotypes of mice viz., C57BL/6 (H-2b) and SWR/J (H-2q). However, preliminary findings revealed no significant change in the total IgG antibody response against OVA, as evaluated by ELISA. These results confirm the suppressive activity of S. nux-vomica on allergen-specific IgE antibody response and suggest its possible application in allergic conditions. <br/> <br/>Page(s): 341-344