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    <title>NISCAIR Online Periodicals Repository Community: IJBB Vol.40 [2003]</title>
    <link>http://nopr.niscair.res.in/handle/123456789/3686</link>
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    <item>
      <title>Hydroxyproline concentrations in ocular tissues of Arabian camel  (Camelus dromedarius Linn.)</title>
      <link>http://nopr.niscair.res.in/handle/123456789/3825</link>
      <description>Title: Hydroxyproline concentrations in ocular tissues of Arabian camel  (Camelus dromedarius Linn.)
&lt;br/&gt;
&lt;br/&gt;Authors: Siddiqi, N J; Alhomida, A S
&lt;br/&gt;
&lt;br/&gt;Abstract: Hydroxyproline (Hyp) concentrations (total, free, peptide-bound and protein-bound) in camel eye tissues were determined. Total Hyp concentration was highest in iris, followed by ciliary body, sclera, cornea, lens and retina; the difference between total Hyp concentration of iris and sclera (P &lt; 0.05) and cornea, lens and retina (P &lt; 0.001) was statistically significant. Cornea had the highest concentration of free Hyp, followed by ciliary body, retina, iris, sclera and lens (P &lt; 0.001). Peptide-bound Hyp concentration was highest in iris, followed by lens, cornea, ciliary body, retina and sclera (P &lt; 0.001). Iris also had the highest concentration of protein-bound Hyp, followed by ciliary body, sclera, cornea, retina and lens; the difference in the protein-bound Hyp concentration between iris and sclera (P &lt; 0.05) and cornea, retina and lens (P &lt; 0.001) was statistically significant. Iris was also found to have the highest concentration of collagen, followed by ciliary body, sclera, cornea, lens and retina; the difference between the collagen concentration of iris and sclera (P &lt; 0.05) and cornea, lens and retina (P &lt; 0.001) was statistically significant. These variations may result from differences in the collagen structure and/or composition in these tissues.
&lt;br/&gt;
&lt;br/&gt;Page(s): 451-454</description>
      <pubDate>Fri, 28 Nov 2003 22:58:59 GMT</pubDate>
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    <item>
      <title>Lipid peroxidation and scavenging enzyme levels in the liver of streptozotocin-induced diabetic rats</title>
      <link>http://nopr.niscair.res.in/handle/123456789/3824</link>
      <description>Title: Lipid peroxidation and scavenging enzyme levels in the liver of streptozotocin-induced diabetic rats
&lt;br/&gt;
&lt;br/&gt;Authors: Bukan, Neslihan; Sancak, Banu; Yavuz, Ozlem; Koca, Cemile; Tutkun, Funda; Ozcelikay, A Tanju; Altan, Nilgun
&lt;br/&gt;
&lt;br/&gt;Abstract: In this study, alterations in the liver antioxidant enzymes status and lipid peroxidation in short-term (8-weeks) and long-term &#xD;
(24-weeks) diabetic rats were examined. Glutathione peroxidase (GSH-Px) activity and malondialdehyde (MDA) levels were significantly increased, but superoxide dismutase (SOD) activity was significantly reduced in 8-weeks diabetic rats, compared to control. Catalase (CAT) activity, however, was found unchanged. In 24-weeks diabetic rats, while GSH-Px activity was unchanged, but SOD and CAT activities and MDA levels were significantly increased, compared to control. These results suggest that diabetes-induced alterations in tissue antioxidant system may reflect a generalized increase in tissue oxidative stress. It can be concluded that lipid peroxidation and antioxidant enzyme levels are elevated in diabetic condition. Hence, diabetes mellitus, if left untreated, may increase degenerative processes due to accumulation of oxidative free radicals.
&lt;br/&gt;
&lt;br/&gt;Page(s): 447-450</description>
      <pubDate>Fri, 28 Nov 2003 22:58:59 GMT</pubDate>
    </item>
    <item>
      <title>Purification of catecholase from Solanum melangena (brinjal)</title>
      <link>http://nopr.niscair.res.in/handle/123456789/3823</link>
      <description>Title: Purification of catecholase from Solanum melangena (brinjal)
&lt;br/&gt;
&lt;br/&gt;Authors: Goswami, Anita P; Amarapurkar, Sudha V
&lt;br/&gt;
&lt;br/&gt;Abstract: Catecholase was purified from cortex of Solanum melangena (brinjal) on natural affiant, lignin. The elution profile showed seven peaks with the 6&lt;sup&gt;th&lt;/sup&gt; peak having 4616-fold purity. The 6&lt;sup&gt;th&lt;/sup&gt; pure fraction loaded on PAGE showed two protein bands on staining with Coomassie brilliant blue, one at the point of application and other near the dye front. These bands exhibited catecholase activity, when stained with 4-methyl catechol and proline, Basic fuschin and ethidium bromide showed positive tests, indicating that catecholase is a ribonucleoglycoprotein.
&lt;br/&gt;
&lt;br/&gt;Page(s): 442-446</description>
      <pubDate>Fri, 28 Nov 2003 22:58:59 GMT</pubDate>
    </item>
    <item>
      <title>Mutation analysis in spinal muscular atrophy using allele-specific polymerase chain reaction</title>
      <link>http://nopr.niscair.res.in/handle/123456789/3822</link>
      <description>Title: Mutation analysis in spinal muscular atrophy using allele-specific polymerase chain reaction
&lt;br/&gt;
&lt;br/&gt;Authors: Kesari, Akanchha; Mukherjee, Monisha; Mittal, Balraj
&lt;br/&gt;
&lt;br/&gt;Abstract: Polymerase chain reaction (PCR), followed by restriction digestion is universally used for molecular diagnosis of spinal muscular atrophy (SMA). In the present study, we have used a modified strategy based on amplification refractory mutation system-polymerase chain reaction (ARMS-PCR) to develop a rapid and reliable method for mutation detection and prenatal diagnosis in SMA patients. The telomeric (SMN1) and centromeric (SMN2) copies of exon 7 of the survival motor neuron (SMN) gene were amplified by ARMS-PCR, using primers specific to SMN1 and SMN2 nucleotide sequence with the exonic mismatch G (for SMN1) and A (for SMN2) at the 3’ end. The PCR products were analyzed on agarose gels. All the patients who had homozygous deletion of exon 7 of SMN1 gene by conventional PCR-restriction fragment length polymorphism (PCR-RFLP) method showed the same deletion status by ARMS-PCR. This procedure showed a 100% concordance between PCR-RFLP and ARMS-PCR methods for the detection of SMN1/SMN2 status in patients with SMA. An artifact due to incomplete digestion is not a problem while using ARMS-PCR. The modified protocol is specific, rapid and highly reliable for use in prenatal diagnosis &#xD;
as well.
&lt;br/&gt;
&lt;br/&gt;Page(s): 439-441</description>
      <pubDate>Fri, 28 Nov 2003 22:58:59 GMT</pubDate>
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