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  <title>NOPR Collection:</title>
  <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19739" />
  <subtitle />
  <id>http://nopr.niscpr.res.in/handle/123456789/19739</id>
  <updated>2026-10-08T13:23:04Z</updated>
  <dc:date>2026-10-08T13:23:04Z</dc:date>
  <entry>
    <title>Role of mouse spleen cell HMG proteins and their poly-ADP-ribosylation in betelnut induced carcinogenesis</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19766" />
    <author>
      <name>Pariat, Theisara</name>
    </author>
    <author>
      <name>Sharan, R N</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19766</id>
    <updated>2013-07-15T16:33:04Z</updated>
    <published>2002-04-01T00:00:00Z</published>
    <summary type="text">Title: Role of mouse spleen cell HMG proteins and their poly-ADP-ribosylation in betelnut induced carcinogenesis
Authors: Pariat, Theisara; Sharan, R N
Abstract: The role of high mobility group (HMG) proteins&#xD;
and their poly-ADP-ribosylation (PAR) in betel nut induced initiation of carcinogenesis&#xD;
in mice has been studied. A known carcinogen, diethylnitrosamine (DEN) was used&#xD;
as a positive control. Swiss albino mice were chronically exposed to aqueous&#xD;
extract of betel nut (AEBN) or DEN at low doses for up to 4 weeks.&#xD;
&#xD;
The poly-ADP-ribosylation (PAR) of spleen&#xD;
cell HMG proteins was monitored using [32P]-NAD+. Parallel to this, chromatin&#xD;
was subjected to DNase I cleavage and the organizational state of the chromatin&#xD;
was monitored. The PAR of HMG proteins showed a marked progressive reduction at&#xD;
different times following AEBN- or DEN treatment. HMG proteins isolated from&#xD;
the control and carcinogen treated mice were allowed to reassociate with the&#xD;
untreated spleen cells chromatin. The reassociated chromatin showed progressive&#xD;
relaxation in its superstructure. The results suggest that under the influence of&#xD;
potential carcinogens AEBN or DEN, the mouse spleen cell HMG proteins created molecular&#xD;
conditions favourable to initiation of cancer.
Page(s): 130-132</summary>
    <dc:date>2002-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Oxidative burden and antioxidant defense system in polymorphonuclear leukocytes of human lung diseases</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19763" />
    <author>
      <name>Sharma, Rashmi N</name>
    </author>
    <author>
      <name>Bhardwaj, A</name>
    </author>
    <author>
      <name>Behera, D</name>
    </author>
    <author>
      <name>Khanduja, K L</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19763</id>
    <updated>2013-07-17T16:32:41Z</updated>
    <published>2002-04-01T00:00:00Z</published>
    <summary type="text">Title: Oxidative burden and antioxidant defense system in polymorphonuclear leukocytes of human lung diseases
Authors: Sharma, Rashmi N; Bhardwaj, A; Behera, D; Khanduja, K L
Abstract: Superoxide anion (O2.&lt;sup&gt;-&lt;/sup&gt;) and&#xD;
hydrogen peroxide (H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt;) production was significantly&#xD;
higher in blood neutrophils (PMNs) of patients with lung cancer and&#xD;
non-malignant lung diseases when compared to the controls (&lt;i&gt;p&lt;/i&gt;&lt;0.001).&#xD;
Superoxide dismutase (SOD) activity was significantly decreased in PMNs of&#xD;
patients with lung cancer (&lt;i&gt;p&lt;/i&gt;&lt;0.00l). Similarly, catalase&#xD;
&#xD;
and glutathione peroxidase (GPx)&#xD;
activities were lower in PMNs of lung cancer patients as compared to&#xD;
non-malignant lung diseases and controls. There was an increase in HMP shunt&#xD;
activity as measured by rate of formation of &lt;sup&gt;14&lt;/sup&gt;CO&lt;sub&gt;2&lt;/sub&gt; from [1-&lt;sup&gt;14&lt;/sup&gt;C]-glucose&#xD;
in PMNs of lung cancer patients. Modifications in the antioxidant defense&#xD;
system in PMNs of malignant and non-malignant lung diseases, the changes being&#xD;
more in the malignancy are indicated.
Page(s): 124-129</summary>
    <dc:date>2002-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Effect of harmaline on rat intestinal brush border sucrase activity</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19762" />
    <author>
      <name>Kaur, Navneet</name>
    </author>
    <author>
      <name>Kaur, Jyotdeep</name>
    </author>
    <author>
      <name>Mahmood, Akhtar</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19762</id>
    <updated>2013-07-15T16:32:51Z</updated>
    <published>2002-04-01T00:00:00Z</published>
    <summary type="text">Title: Effect of harmaline on rat intestinal brush border sucrase activity
Authors: Kaur, Navneet; Kaur, Jyotdeep; Mahmood, Akhtar
Abstract: The effect of harmaline, a plant alkaloid&#xD;
has been studied on rat intestinal brush border sucrase activity. Stimulation of&#xD;
sucrase activity by Na+ was found to be &lt;i&gt;p&lt;/i&gt;H-dependent. At neutral &lt;i&gt;p&lt;/i&gt;H&lt;i&gt;,&#xD;
&lt;/i&gt;20 m&lt;i&gt;M&lt;/i&gt; Na&lt;sup&gt;+&lt;/sup&gt; stimulated sucrase activity by reducing &lt;i&gt;K&lt;/i&gt;&lt;sub&gt;m&lt;/sub&gt;&lt;i&gt;&#xD;
&lt;/i&gt;by 30%&lt;i&gt; &lt;/i&gt;while at acidic &lt;i&gt;p&lt;/i&gt;H&lt;i&gt; &lt;/i&gt;(5.2), the activity&#xD;
increased 4-fold compared to Na&lt;sup&gt;+&lt;/sup&gt;-free enzyme. At 1.0 m&lt;i&gt;M&lt;/i&gt;,&#xD;
harmaline&#xD;
&#xD;
markedly inhibited (67%)&lt;i&gt; &lt;/i&gt;the&#xD;
enzyme activity at &lt;i&gt;p&lt;/i&gt;H&lt;i&gt; &lt;/i&gt;5.2 in the absence of Na&lt;sup&gt;+&lt;/sup&gt;.&#xD;
However, inhibition was reduced in presence of 20 m&lt;i&gt;M&lt;/i&gt; sodium, whereas 4.0&#xD;
m&lt;i&gt;M&lt;/i&gt; harmaline was required to inhibit the enzyme activity by 65%&lt;i&gt;. &lt;/i&gt;In&#xD;
the absence of Na&lt;sup&gt;+&lt;/sup&gt; ions, harmaline inhibition of sucrase activity&#xD;
was of competitive type, but it changed to non-competitive type in presence of 20&lt;i&gt;&#xD;
m&lt;/i&gt;M&lt;i&gt; &lt;/i&gt;Na&lt;sup&gt;+&lt;/sup&gt; at &lt;i&gt;p&lt;/i&gt;H&lt;i&gt; &lt;/i&gt;5.2. Sucrase-harmaline&#xD;
interactions as a function of &lt;i&gt;p&lt;/i&gt;H&lt;i&gt;, &lt;/i&gt;both in presence and absence of&#xD;
Na&lt;sup&gt;+&lt;/sup&gt; revealed a shift in &lt;i&gt;p&lt;/i&gt;H&lt;i&gt; &lt;/i&gt;optima of the enzyme&#xD;
towards a higher &lt;i&gt;p&lt;/i&gt;H&lt;i&gt; &lt;/i&gt;in presence of 4 m&lt;i&gt;M&lt;/i&gt; and 1 m&lt;i&gt;M&lt;/i&gt;&#xD;
harmaline respectively. The observed inhibition was reversible in nature and was&#xD;
only partially overcome by sodium, lithium, potassium, cesium, rubidium and ammonium&#xD;
ions. These findings suggest that harmaline also inhibits rat brush border sucrase&#xD;
and that the presence of Na&lt;sup&gt;+&lt;/sup&gt; site is not a pre-requisite for the&#xD;
inhibition.
Page(s): 119-123</summary>
    <dc:date>2002-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Characterization of a 59 kDa gelatin-binding fragment of buffalo plasma fibronectin</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19761" />
    <author>
      <name>Ahmed, Nizamuddin</name>
    </author>
    <author>
      <name>Swamy, Naganath</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19761</id>
    <updated>2013-07-17T16:32:30Z</updated>
    <published>2002-04-01T00:00:00Z</published>
    <summary type="text">Title: Characterization of a 59 kDa gelatin-binding fragment of buffalo plasma fibronectin
Authors: Ahmed, Nizamuddin; Swamy, Naganath
Abstract: Limited proteolysis of buffalo plasma fibronectin&#xD;
(FN) by thermolysin yielded four gelatin-binding fragments of which, the major 59&#xD;
kDa fragment, GBFl, was isolated by gelatin-Sepharose and heparin-Sepharose&#xD;
affinity columns. GBFl appeared during early phase of thermolysin digestion and&#xD;
remained intact even after 4 hr of digestion. GBF1 may be similar to 56 kDa&#xD;
gelatin-binding fragment of FNs from human and hamster plasma. But, it is more&#xD;
resistant to thermolysin cleavage. The fragment binds to heparin with low affinity.&#xD;
On the basis of the structure of human plasma FN, the modular structure of GBFl&#xD;
may be given as: &lt;sup&gt;6&lt;/sup&gt;Fn1 &lt;sup&gt;1&lt;/sup&gt;Fn2 &lt;sup&gt;2&lt;/sup&gt;Fn2 &lt;sup&gt;7&lt;/sup&gt;Fn1&#xD;
&lt;sup&gt;8&lt;/sup&gt;Fn1 &lt;sup&gt;9&lt;/sup&gt;Fnl &lt;sup&gt;1&lt;/sup&gt;Fn3. Biophysical properties of GBF1&#xD;
suggest an expanded native conformation. The interaction of the fragment with gelatin&#xD;
is &lt;i&gt;p&lt;/i&gt;H-dependent and independent of NaCl concentration.
Page(s): 113-118</summary>
    <dc:date>2002-04-01T00:00:00Z</dc:date>
  </entry>
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