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    <title>NISCAIR Online Periodicals Repository Collection: IJBB Vol.46(4) [August 2009]</title>
    <link>http://nopr.niscair.res.in/handle/123456789/5793</link>
    <description />
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        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/5804" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/5803" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/5802" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/5801" />
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    <title>The Collection's search engine</title>
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  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/5804">
    <title>Serum biochemical markers in rheumatoid arthritis</title>
    <link>http://nopr.niscair.res.in/handle/123456789/5804</link>
    <description>Title: Serum biochemical markers in rheumatoid arthritis
&lt;br/&gt;
&lt;br/&gt;Authors: Pallinti, Vasanthi; Ganesan, Nalini; Anbazhagan, M; Rajasekhar, G
&lt;br/&gt;
&lt;br/&gt;Abstract: &lt;smarttagtype namespaceuri="urn:schemas-microsoft-com:office:smarttags" name="place" downloadurl="http://www.5iantlavalamp.com/"&gt;&lt;smarttagtype namespaceuri="urn:schemas-microsoft-com:office:smarttags" name="City" downloadurl="http://www.5iamas-microsoft-com:office:smarttags"&gt; Rheumatoid arthritis (RA) characterized by local and systemic effects of inflammation has a wide range of biochemical markers implicated directly or indirectly to its pathogenesis. In the present study, homocysteine, cortisol, adenosine deaminase (ADA), ferritin, malondialdehyde (MDA) and &lt;img src='/image/spc_char/alpha.gif'&gt;-tocopherol in serum of RA patients and healthy individuals were estimated to assess if they contribute to the disease process. The markers of disease activity such as erythrocyte sedimentation rate (ESR) and rheumatoid factor (RF) were also measured. The study group included a total of 45 subjects, including 30 RA patients and the rest being healthy individuals. RA group showed a significant increase in the levels of homocysteine, ADA and MDA, and a significant decrease in α-tocopherol compared to the healthy individuals. However, cortisol and ferritin levels did not show any significant change. Also, there was no significant correlation between the studied serum markers and markers of disease activity. Our results indicate that these biochemical markers contribute independently to the pathogenesis of RA. &lt;/smarttagtype&gt;&lt;/smarttagtype&gt;
&lt;br/&gt;
&lt;br/&gt;Page(s): 342-344</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/5803">
    <title>Purification and characterization of bacteriocin produced by strain of &lt;i style=""&gt;Lactobacillus brevis&lt;/i&gt; MTCC 7539</title>
    <link>http://nopr.niscair.res.in/handle/123456789/5803</link>
    <description>Title: Purification and characterization of bacteriocin produced by strain of &lt;i style=""&gt;Lactobacillus brevis&lt;/i&gt; MTCC 7539
&lt;br/&gt;
&lt;br/&gt;Authors: Gautam, Neha; Sharma, Nivedita
&lt;br/&gt;
&lt;br/&gt;Abstract: Bacteriocin, an antimicrobial agent having potential for food biopreservation was purified from&lt;i style=""&gt; Lactobacillus brevis &lt;/i&gt;(a safe food-grade bacteria isolated from &lt;i&gt;Vari Kandal&lt;/i&gt;, a traditional fermented food of Himachal Pradesh by adopting a novel repeated washing method. Its purity was confirmed by SDS-PAGE and Native-PAGE. The relative molecular mass of bacteriocin was 93.74 kD, while specific activity and recovery were 35.52 folds and 17.13%, respectively. It showed high thermal stability and was active over wide range of pH and exhibited sensitivity to trypsin.
&lt;br/&gt;
&lt;br/&gt;Page(s): 337-341</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/5802">
    <title>Effect of nickel on root growth and the kinetics of metal ions transport in onion (&lt;i style=""&gt;Allium cepa&lt;/i&gt;) root</title>
    <link>http://nopr.niscair.res.in/handle/123456789/5802</link>
    <description>Title: Effect of nickel on root growth and the kinetics of metal ions transport in onion (&lt;i style=""&gt;Allium cepa&lt;/i&gt;) root
&lt;br/&gt;
&lt;br/&gt;Authors: Akbaş, Halide; Dane, Feruzan; Meriç, Çiler
&lt;br/&gt;
&lt;br/&gt;Abstract: &lt;smarttagtype namespaceuri="urn:schemas-microsoft-com:office:smarttags" name="metricconverter"&gt; The effect of different concentrations of nickel nitrate (0.25, 0.50, 1.00 and 2.00 m&lt;i style=""&gt;M&lt;/i&gt;) uptake by the roots&lt;b style=""&gt;,&lt;/b&gt; on root growth of onion (&lt;i style=""&gt;Allium cepa&lt;/i&gt;) and the transport of Ni&lt;sup&gt;2+&lt;/sup&gt;, Fe&lt;sup&gt;2+&lt;/sup&gt;, Mn&lt;sup&gt;2+&lt;/sup&gt;, Zn&lt;sup&gt;2+&lt;/sup&gt;, K&lt;sup&gt;+&lt;/sup&gt;, Na&lt;sup&gt;+&lt;/sup&gt; and H&lt;sup&gt;+&lt;/sup&gt; ions were investigated spectrophotometrically. The uptake of Ni&lt;sup&gt;2+&lt;/sup&gt;,&lt;sup&gt; &lt;/sup&gt;Fe&lt;sup&gt;2+&lt;/sup&gt;, Mn&lt;sup&gt;2+&lt;/sup&gt; and Zn&lt;sup&gt;2+&lt;/sup&gt; was monitored by flame atomic absorption spectrometry with a 24-h period for 7 days and the amounts of K&lt;sup&gt;+&lt;/sup&gt; and Na&lt;sup&gt;+&lt;/sup&gt; were determined in solutions by flame photometer. The mineral content of the solution, instead of the root material was measured. Ni&lt;sup&gt;2+&lt;/sup&gt; ions showed inhibitory effect on the root growth at all concentrations during the entire treatment. The EC&lt;sub&gt;50 &lt;/sub&gt;(effective concentration that reduced root growth by 50%) was found at 0.25 m&lt;i style=""&gt;M&lt;/i&gt; Ni&lt;sup&gt;2+&lt;/sup&gt;. No significant change in inhibitory effect was observed after at 0.50 m&lt;i style=""&gt;M&lt;/i&gt;&lt;b style=""&gt; &lt;/b&gt;Ni&lt;sup&gt;2+ &lt;/sup&gt;concentrations. A large amount of Ni&lt;sup&gt;2+&lt;/sup&gt; was translocated into the roots. The kinetics of metal ion transport followed a pseudo-first order reaction in all metal ion concentrations. Ni&lt;sup&gt;2+&lt;/sup&gt;, Zn&lt;sup&gt;2+ &lt;/sup&gt;Fe&lt;sup&gt;2+ &lt;/sup&gt;Mn&lt;sup&gt;2+&lt;/sup&gt; and H&lt;sup&gt;+&lt;/sup&gt; ions transferred together into plant, but Na&lt;sup&gt;+&lt;/sup&gt; and K&lt;sup&gt;+&lt;/sup&gt; ions transferred to the solution from the plant. The amount of H&lt;sup&gt;+&lt;/sup&gt; in the solution decreased at all Ni&lt;sup&gt;2+ &lt;/sup&gt;concentrations. &lt;/smarttagtype&gt;
&lt;br/&gt;
&lt;br/&gt;Page(s): 332-336</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/5801">
    <title>Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement</title>
    <link>http://nopr.niscair.res.in/handle/123456789/5801</link>
    <description>Title: Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement
&lt;br/&gt;
&lt;br/&gt;Authors: Mathavan, Vinodaran M K; Boh, Boon Kim; Tayyab, Saad
&lt;br/&gt;
&lt;br/&gt;Abstract: The interaction of erythrosine B (ErB), a commonly used dye for coloring foods and drinks, with bovine serum albumin (BSA) was investigated both in the absence and presence of bilirubin (BR) using absorption and absorption difference spectroscopy. ErB binding to BSA was reflected from a significant red shift of 11 nm in the absorption maximum of ErB (527 nm) with the change in absorbance at λ&lt;sub&gt;max&lt;/sub&gt;. Analysis of absorption difference spectroscopic titration results of BSA with increasing concentrations of ErB using Benesi-Hildebrand equation gave the association constant, &lt;i style=""&gt;K &lt;/i&gt;as 6.9 &lt;img src='/image/spc_char/cross.gif'&gt; 10&lt;sup&gt;4&lt;/sup&gt; M&lt;sup&gt;-1&lt;/sup&gt;. BR displacing action of ErB was revealed by a significant blue shift in the absorption maximum, accompanied by a decrease in absorbance difference at λ&lt;sub&gt;max&lt;/sub&gt; in the difference spectrum of BR-BSA complex upon addition of increasing concentrations of ErB. This was further substantiated by fluorescence spectroscopy, as addition of increasing concentrations of ErB to BR-BSA complex caused a significant decrease in fluorescence at 510 nm. The results suggest that ErB binds to a site in the vicinity of BR binding site on BSA. Therefore, intake of ErB may increase the risk of hyperbilirubinemia in the healthy subjects.
&lt;br/&gt;
&lt;br/&gt;Page(s): 325-331</description>
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