01934nas a2200229   4500008004100000022001400041245014900055210006900204260009700273300001200370490000800382520099300390653002101383653002601404653002201430653002801452653002801480100002701508700001301535700002601548856013001574       2009                        eng d  a0944-501300aPurification and characterization of putative alkaline [Ni-Fe] hydrogenase from unicellular marine green alga, tetraselmis kochinensis NCIM 16050 aPurification and characterization of putative alkaline NiFe hydr  aOFFICE JENA, P O BOX 100537, 07705 JENA, GERMANYbELSEVIER GMBH, URBAN & FISCHER VERLAGcFEB  a131-1370 v1643 a<p>Hydrogenase enzyme from the unicellular marine green alga Tetraselmis kochinensis NCIM 1605 was purified 467 fold to homogeneity. The molecular weight was estimated to be similar to 89kDa by SDS-PAGE. This enzyme consists of two subunits with molecular masses of similar to 70 and similar to 19 kDa. The hydrogenase was found to contain 10 g atoms of Fe and 1 g of atom of Ni per mote of protein. The specific activity of hydrogen evolution was 50 mu mol H-2/mg/h of enzyme using reduced methyl viologen as an electron donor. This hydrogenase enzyme has pl value similar to 9.6 representing its alkaline nature. The absorption spectrum of the hydrogenase enzyme showed an absorption peak at 425 nm indicating that the enzyme had iron-sulfur clusters. The total of 16 cysteine residues were found per mote of enzyme under the denaturing condition and 20 cysteine residues in reduced denatured enzyme indicating that it has two disulfide bridges. (C) 2007 Published by Elsevier GmbH.</p>10aCharacterization10aChemical modification10aNi-Fe hydrogenase10aTetraselmis kochinensis10aUnicellular green algae1 aBhosale, Siddharth, H.1 aPant, A.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/purification-and-characterization-putative-alkaline-ni-fe-hydrogenase-unicellular-marine-002225nas a2200241   4500008004100000022001400041245009500055210006900150260010000219300001200319490000700331520133700338653001501675653001901690653002601709653002401735100002701759700001801786700002501804700001701829700001901846856011801865       2011                        eng d  a0254-870400aActive pharmaceutical ingredient (api) from an estuarine fungus, microdochium nivale (Fr.)0 aActive pharmaceutical ingredient api from an estuarine fungus mi  aC/O KIRAN DALELA, 1/206 VIKAS NAGAR, KURSI RD, LUCKNOW 226 022, INDIAbTRIVENI ENTERPRISEScSEP  a653-6580 v323 a<p>Various marine habitats sustain variety of bio-sources of ecological and biotech potentials. Pharmaceutical potential compound Cyclosporine A was reported from marine fungus Microdochium nivale associated with Porteresia coarctata, a marine salt marsh grass from mangrove environment distributed along the Central West Coast (CWC) of India. This study involves association of M. nivale with P. coarctata plant, fermentation conditions, purification of Cyclosporine A, chemical characterization etc. Its antifungal inhibition and MIC (Minimum inhibitory concentration) against Aspergillus strains (A. niger, A. japonicus, A. fresenii), yeasts and dermatophytes (Candida sp., Cryptococcus neoformans, Trichophyton mentagrophytes, T tonsurans, T violaceum, Microsporium gypsum and Fusarium sp.) were evaluated. However, the MIC against A. japonicus, C. neoformans, Candida sp. and T. tonsurans were confirmed to be as low as 12.5-25 mg disc(-1). The antifungal properties of Cyclosporine A against Aspergillus species, yeast and dermatophytes revealed that Cyclosporine A would be a potential compound for life threatening diseases caused by above fungi in both human and animals. Furthermore, we have reported herewith another source of Cyclosporin A derived from filamentous fungus, M. nivale. occurring in marine environment.</p>10aantifungal10aCyclosporine A10aEstuarine environment10aMicrodochium nivale1 aBhosale, Siddharth, H.1 aPatil, K., B.1 aParameswaran, P., S.1 aNaik, C., G.1 aJagtap, T., G.  uhttps://library.ncl.res.in/content/active-pharmaceutical-ingredient-api-estuarine-fungus-microdochium-nivale-fr-001853nas a2200265   4500008004100000022001400041245011100055210006900166260006900235300001000304490000800314520088600322653002701208653005001235653001501285653001801300653002201318653001501340100001701355700001801372700002701390700001901417700002001436856013101456       2011                        eng d  a1011-134400aFluorescence resonance energy transfer from tryptophan to folic acid in micellar media and deionised water0 aFluorescence resonance energy transfer from tryptophan to folic   aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcAPR  a16-210 v1033 a<p>The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueous sodiumdodecyl sulphate, cetyltrimethyl ammonium bromide, and Brij-35 as well as deionised water was investigated using steady state and time resolved fluorescence techniques. The data obtained from steady state fluorescence spectral studies and time resolved measurement indicated that the FRET from Trp to FA occurred most effectively in aqueous sodium dodecyl sulphate micellar solutions. The distance between Trp and FA were evaluated. Binding constant, number of binding sites and thermodynamic parameters were determined for Trp-FA interactions in deionised water. The values of the thermodynamic parameters suggest that the hydrophobic forces and hydrogen bonding are the key interacting forces between Trp-FA interaction. (C) 2011 Elsevier B.V. All rights reserved.</p>10aFluorescence quenching10aFluorescence resonance energy transfer (FRET)10aFolic acid10aFoster theory10aStern-Volmer plot10aTryptophan1 aMote, U., S.1 aPatil, S., R.1 aBhosale, Siddharth, H.1 aHan, Sung-Hwan1 aKolekar, G., B.  uhttps://library.ncl.res.in/content/fluorescence-resonance-energy-transfer-tryptophan-folic-acid-micellar-media-and-deionised-002631nas a2200277   4500008004100000022001400041245015800055210006900213260007500282300001200357490000700369520154700376653002801923653002201951653002901973653001902002653004802021100002102069700001902090700002702109700002102136700001902157700002502176700002102201856013102222       2012                        eng d  a1053-050900aConformational transitions of the catalytic domain of heme-regulated eukaryotic initiation factor 2 alpha kinase, a key translational regulatory molecule0 aConformational transitions of the catalytic domain of hemeregula  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScJAN  a431-4410 v223 a<p>In mammalian cells, the heme-regulated inhibitor (HRI) plays a critical role in the regulation of protein synthesis at the initiation step through phosphorylation of a-subunit of the eukaryotic initiation factor 2 (eIF2). In this study we have cloned and performed biophysical characterization of the kinase catalytic domain (KD) of rabbit HRI. The KD described here comprises kinase 1, the kinase insertion domain (KI) and kinase 2. We report here the existence of an active and stable monomer of HRI (KD). The HRI (KD) containing three tryptophan residues was examined for its conformational transitions occurring under various denaturing conditions using steady-state and time-resolved tryptophan fluorescence, circular dichroism (CD) and hydrophobic dye binding. The parameter A and phase diagram analysis revealed multi-state unfolding and existence of three stable intermediates during guanidine hydrochloride (Gdn-HCl) induced unfolding of HRI (KD). The protein treated with 6 M Gdn-HCl showed collisional and static mechanism of acrylamide quenching and the constants (K-sv=3.08 M-1 and K-s=5.62 M-1) were resolved using time resolved fluorescence titration. Based on pH, guanidine hydrochloride and temperature mediated transitions, HRI (KD) appears to exemplify a rigid molten globule-like intermediate with compact secondary structure, altered tertiary structure and exposed hydrophobic patches at pH 3.0. The results indicate the inherent structural stability of HRI (KD), a member of the class of stress response proteins.</p>10aCircular dichroism (CD)10aeIF2 alpha kinase10aHeme-regulated inhibitor10aMolten globule10aSteady-state and time-resolved fluorescence1 aSreejith, R., K.1 aSuresh, C., G.1 aBhosale, Siddharth, H.1 aBhavnani, Varsha1 aKumar, Avinash1 aGaikwad, Sushama, M.1 aPal, Jayanta, K.  uhttps://library.ncl.res.in/content/conformational-transitions-catalytic-domain-heme-regulated-eukaryotic-initiation-factor-2-002227nas a2200265   4500008004100000022001400041245014100055210006900196260007300265300001200338490000700350520126500357653001201622653001701634653001401651100001701665700002101682700002201703700001801725700001901743700001701762700002701779700002501806856013001831       2015                        eng d  a0141-813000aZinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity0 aZinc inhibits glycation induced structural functional modificati  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAUG  a601-6100 v793 a<p>The present work aims to investigate the concentration and time dependant effect of zinc on the in vitro non enzymatic modifications of albumin by diabetic levels of glucose. Further, preventive and curative effect of zinc was studied by adding zinc before and after initiation of glycation respectively. Glycation of albumin was done at different concentrations of zinc (125, 250 and 500 mu M) at different time intervals (21,28 and 35 days) with appropriate controls. The antiglycation potential of zinc was assessed by estimating different markers of albumin glycation (fructosamines, carbonyls, bound sugar, AGEs), structural modifications (free amino, thiol group, beta amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 mu M) significantly reduced modifications of albumin which was comparable to aminoguanidine and also protected secondary and tertiary structure of albumin after 28 days of incubation. Zinc exhibited significant protective effect on erythrocytes by inhibiting hemolysis. Thus the present study indicate preventive mode of albumin glycation inhibition by zinc. (C) 2015 Elsevier B.V. All rights reserved.</p>10aAlbumin10aErythrocytes10aGlycation1 aTupe, Rashmi1 aKulkarni, Amruta1 aAdeshara, Krishna1 aSankhe, Neena1 aShaikh, Shamim1 aDalai, Sayli1 aBhosale, Siddharth, H.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/zinc-inhibits-glycation-induced-structural-functional-modifications-albumin-and-protects-002418nas a2200253   4500008004100000022001400041245010700055210006900162260007300231300001200304490000700316520147800323653001601801653002001817653002701837653004101864653001401905100002101919700001801940700002701958700002701985700002502012856012702037       2016                        eng d  a0141-813000aFunctional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera0 aFunctional and conformational transitions of mevalonate diphosph  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a160-1700 v833 a<p>Functional and conformational transitions of mevalonate diphosphate decarboxylase (MDD), a key enzyme of mevalonate pathway in isoprenoid biosynthesis, from Bacopa monniera (BmMDD), cloned and overexpressed in Escherichia coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and Circular dichroism spectroscopy. Native BmMDD is a helix dominant structure with 45% helix and 11% sheets and possesses seven tryptophan residues with two residues exposed on surface, three residues partially exposed and two situated in the interior of the protein. Thermal denaturation of BmMDD causes rapid structural transitions at and above 40 degrees C and transient exposure of hydrophobic residues at 50 degrees C, leading to aggregation of the protein. An acid induced molten globule like structure was observed at pH 4, exhibiting altered but compact secondary structure, distorted tertiary structure and exposed hydrophobic residues. The molten globule displayed different response at higher temperature and similar response to chemical denaturation as compared to the native protein. The surface tryptophans have predominantly positively charged amino acids around them, as indicated by higher K-SV for IC as compared to that for CsCl. The native enzyme displayed two different lifetimes, vi (1.203 +/- 0.036 ns) and tau 2 (3.473 +/- 0.12 ns) indicating two populations of tryptophan. (C) 2015 Elsevier B.V. All rights reserved.</p>10aAggregation10aCD spectroscopy10aFluorescence quenching10aMevalonate diphosphate decarboxylase10aUnfolding1 aShakeel, Abbassi1 aPatel, Krunal1 aKhan, Bashir, Mohammad1 aBhosale, Siddharth, H.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/functional-and-conformational-transitions-mevalonate-diphosphate-decarboxylase-bacopa-0