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    <title>NISCAIR Online Periodicals Repository Collection: IJEB Vol.44(03) [March 2006]</title>
    <link>http://nopr.niscair.res.in/handle/123456789/6313</link>
    <description />
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        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/6986" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/6415" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/6414" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/6413" />
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  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/6986">
    <title>Cytosolic sulfotransferases</title>
    <link>http://nopr.niscair.res.in/handle/123456789/6986</link>
    <description>Title: Cytosolic sulfotransferases
&lt;br/&gt;
&lt;br/&gt;Authors: Nimmagadda, Deepthi; Cherala, Ganesh; Ghatta, Srinivas
&lt;br/&gt;
&lt;br/&gt;Abstract: Sulfoconjugation (Sulfation or Sulfonation) is an important&#xD;
reaction in the phase II biotransformation of a wide number of endogenous and&#xD;
foreign chemicals, including: drugs, toxic chemicals, hormones, and neurotransmitters.&#xD;
The reaction is catalyzed by the members of the cytosolic sulfotransferase&#xD;
(SULT) superfamily, consisting of ten functional genes in humans. Sulfation&#xD;
reaction in living cells is reversed by sulfatase, which hydrolyses the&#xD;
sulfonated conjugates. It has a major role in regulating the endocrine status&#xD;
of an individual by modulating the activity of steroid hormones, their&#xD;
biosynthesis, and the metabolism of catecholamines. Sulfonation is a key&#xD;
reaction in the body's ‘chemical’ defense against xenobiotics. Although the&#xD;
primary function of sulfoconjugation is to permit detoxification of the&#xD;
compound, it also results in the activation of chemical procarcinogens, such as&#xD;
certain dietary and environmental agents into carcinogens. In this review, we&#xD;
summarize our current understanding of the structure of mammalian cytosolic&#xD;
sulfotransferases and their role in human steroid associated cancers and in the&#xD;
bioactivation of chemical carcinogens.
&lt;br/&gt;
&lt;br/&gt;Page(s): 171-182</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/6415">
    <title>Constitutive acetonitrile hydrolysing activity of &lt;i style=""&gt;Nocardia globerula &lt;/i&gt;NHB-2: Optimization of production and reaction conditions</title>
    <link>http://nopr.niscair.res.in/handle/123456789/6415</link>
    <description>Title: Constitutive acetonitrile hydrolysing activity of &lt;i style=""&gt;Nocardia globerula &lt;/i&gt;NHB-2: Optimization of production and reaction conditions
&lt;br/&gt;
&lt;br/&gt;Authors: Kumar, H; Prasad, S; Raj, J; Bhalla, T C
&lt;br/&gt;
&lt;br/&gt;Abstract: &lt;i style=""&gt;Nocardia&#xD;
globerula &lt;/i&gt;NHB-2 exhibited an intracellular&#xD;
acetonitrile hydrolysing activity (AHA) when cultivated in nutrient broth&#xD;
supplemented with glucose (10.0 g/l) and yeast extract (1.0 g/l), at &lt;i style=""&gt;p&lt;/i&gt;H 8.0, 30°C for 21 hr. Maximum AHA was recorded in the culture containing 0.1 &lt;i style=""&gt;M&lt;/i&gt; of sodium phosphate buffer, (&lt;i style=""&gt;p&lt;/i&gt;H 8.8) at 45°C for 15 min with 600 μmol of acetonitrile and resting cells of &lt;i style=""&gt;N. globerula &lt;/i&gt;NHB-2 equivalent to 1.0 ml&#xD;
culture broth. This activity was stable up to 40°C and was completely inactivated at or above 60°C. About five-fold increase in AHA was observed after optimization&#xD;
of culture and reaction conditions. Under the optimized conditions, this&#xD;
organism hydrolyzed various nitriles and amides such as propionitrile,&#xD;
benzonitrile, acetamide, and acrylamide to corresponding acids. This&#xD;
nitrile/amide hydrolysing activity of &lt;i style=""&gt;N.&#xD;
globerula &lt;/i&gt;NHB-2 has potential applications in enzymatic synthesis of&#xD;
organic acids and bioremediation of nitriles and amides contaminated soil and&#xD;
water system.
&lt;br/&gt;
&lt;br/&gt;Page(s): 240-245</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/6414">
    <title>Host range nodulation and adaptation in frenchbean rhizobia</title>
    <link>http://nopr.niscair.res.in/handle/123456789/6414</link>
    <description>Title: Host range nodulation and adaptation in frenchbean rhizobia
&lt;br/&gt;
&lt;br/&gt;Authors: Dhar, B; Mishra, Ashok; Singh, M K
&lt;br/&gt;
&lt;br/&gt;Abstract: The host range nodulation efficiency of four&#xD;
genetically marked frenchbean rhizobial strains (HURR-3, Raj-2, Raj-5 and&#xD;
Raj-6) was studied with five legume hosts namely, frenchbean (&lt;i style=""&gt;Phageolus vulgaris&lt;/i&gt; L.), pigeonpea [&lt;i style=""&gt;Cajanus cajan&lt;/i&gt; (L.) Millsp.], mungbean [&lt;i style=""&gt;Vigna radiata&lt;/i&gt; (L.) Wilezek.], urdbean [&lt;i style=""&gt;Vigna mungo&lt;/i&gt; (L.) Hepper.] and soybean [&lt;i style=""&gt;Glycine max&lt;/i&gt; (L.) Merril.]. Except&#xD;
soybean and pigeonpea, all other legume hosts were nodulated by two or more&#xD;
frenchbean rhizobial strains tested. Rhizobia were isolated from nodules&#xD;
produced by strains, HURR-3 and Raj-5, on main (frenchbean) and different&#xD;
(mungbean and urdbean) hosts. There was marked improvement in host range&#xD;
nodulation and nitrogen fixation efficiency of rhizobial strains, HURR-3 and&#xD;
Raj-5, after their isolation from chance nodules on different hosts. This is&#xD;
clearly evident from the ability of such isolates to form nodules on pigeonpea&#xD;
besides mungbean and urdbean, and higher nodulation in all the above three&#xD;
different hosts. The phage-susceptibility pattern and intrinsic antibiotic&#xD;
resistance (used as markers) of the two strains did not change after their&#xD;
passage through different hosts. The results indicate that frenchbean rhizobia&#xD;
had undergone some modification in symbiotic behaviour to adapt to wide host&#xD;
range during their passage through different (alternate?) hosts.
&lt;br/&gt;
&lt;br/&gt;Page(s): 250-253</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/6413">
    <title>Optimum conditions for L-glutaminase production by actinomycete strain isolated from estuarine fish,&lt;i style=""&gt; Chanos chanos &lt;/i&gt;(Forskal, 1775)</title>
    <link>http://nopr.niscair.res.in/handle/123456789/6413</link>
    <description>Title: Optimum conditions for L-glutaminase production by actinomycete strain isolated from estuarine fish,&lt;i style=""&gt; Chanos chanos &lt;/i&gt;(Forskal, 1775)
&lt;br/&gt;
&lt;br/&gt;Authors: Sivakumar, K; Sahu, Maloy Kumar; Manivel, P R; Kannan, L
&lt;br/&gt;
&lt;br/&gt;Abstract: Actinomycetes were isolated from skin, gills&#xD;
and gut contents of estuarine fish, &lt;i style=""&gt;Chanos&#xD;
chanos &lt;/i&gt;using Kuster’s agar medium. Out of 20 strains tested, the strain&#xD;
LG-10 which was tentatively identified as &lt;i style=""&gt;Streptomyces&#xD;
rimosus&lt;/i&gt; showed L-glutaminase activity. Optimum production of L-glutaminase&#xD;
enzyme (17.51 IU/ml) was observed after 96 h of incubation at 27° C, &lt;i style=""&gt;p&lt;/i&gt;H 9 and glucose and&#xD;
malt extract as carbon and nitrogen sources, respectively. The present study&#xD;
indicated scope for the use of &lt;i style=""&gt;S. rimosus&#xD;
&lt;/i&gt;as an ideal organism for the industrial production of extracellular&#xD;
L-glutaminase.
&lt;br/&gt;
&lt;br/&gt;Page(s): 256-258</description>
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