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    <title>NOPR Collection:</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/28661</link>
    <description />
    <pubDate>Sat, 10 Oct 2026 20:10:40 GMT</pubDate>
    <dc:date>2026-10-10T20:10:40Z</dc:date>
    <item>
      <title>A study on human leukocyte antigen class I molecules in paediatric bronchial asthma</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/28695</link>
      <description>Title: A study on human leukocyte antigen class I molecules in paediatric bronchial asthma
Authors: Mishra, Mahendra N; Dudeja, Puja; Gupta, Rakesh K
Abstract: Childhood&#xD;
asthma, often associated with atopy, is more common in boys and may persist&#xD;
throughout life in 50% of cases.&lt;b&gt; &lt;/b&gt;This case-control study was carried out to examine if any association of paediatric bronchial asthma with human&#xD;
leukocyte antigen (HLA) class I antigens. Thirty-six children with bronchial&#xD;
asthma diagnosed on basis of Global Initiative for Asthma (GINA) criteria and&#xD;
an equal number of healthy controls without&#xD;
history of bronchial asthma were studied. Low resolution &#xD;
HLA- ABC typing was performed by sequence specific primers (SSP) and the&#xD;
frequency of HLA–ABC antigens in the two groups was compared. Total serum&#xD;
immunoglobulin E (IgE) estimation was done as a marker of atopy by ELISA. The&#xD;
study included 24 boys and 12 girls aged 13 months to 11 yrs, of which 16 (44%)&#xD;
had positive family history. Serum IgE levels were elevated in 20 (55%) of the&#xD;
cases and 33% of controls with peak values of 4877 and 627 IU/ml, respectively.&#xD;
No statistically significant correlation was observed between childhood asthma&#xD;
and HLA class I antigens, however, a statistically significant correlation was&#xD;
observed between serum IgE levels and asthma, which was elevated in cases, as&#xD;
compared to normal population. Serum IgE levels did not show a linear trend, in&#xD;
that a direct correlation with the severity of disease was not observed.
Page(s): 160-163</description>
      <pubDate>Tue, 01 Apr 2014 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/28695</guid>
      <dc:date>2014-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>Effect of gold nanoparticles on superoxide dismutase and indoleamine 2, 3-dioxygenase in various rat tissues</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/28694</link>
      <description>Title: Effect of gold nanoparticles on superoxide dismutase and indoleamine 2, 3-dioxygenase in various rat tissues
Authors: Siddiqi, N J
Abstract: Gold&#xD;
nanoparticles have diverse applications and are being used in food and cosmetic&#xD;
industry, for drug delivery and in the diagnosis and treatment of cancer.&#xD;
However there is a need to study their biochemical mode of action. In this&#xD;
study, &lt;i&gt;in vivo&lt;/i&gt; effect of gold nanoparticles on the activities of the two&#xD;
antioxidant enzymes — superoxide dismutase (SOD) and indoleamine&#xD;
2,3-dioxygenase (IDO) was investigated in various tissues of rats. Rats were&#xD;
injected with 20 μg/kg body wt of 20 nm gold nanoparticles for three&#xD;
consecutive days through intraperitoneal route. The animals were sacrificed by&#xD;
CO&lt;sub&gt;2&lt;/sub&gt; asphyxiation 24 h after the last dose of gold nanoparticles.&#xD;
Results showed that treatment with gold nanoparticles caused no significant change&#xD;
in SOD activity in most of the tissues, except kidneys. In kidneys, gold&#xD;
nanoparticles caused a significant increase in SOD activity, when compared to&#xD;
the activity in control rats. However, treatment with gold nanoparticles&#xD;
altered the expression pattern of SOD activity in various tissues. For example,&#xD;
in control rats highest SOD activity was demonstrated in heart and least in&#xD;
kidneys and spleen. But, in gold nanoparticles treated rats, maximum SOD&#xD;
activity was observed in liver and the lowest in spleen. Gold nanoparticles&#xD;
caused no significant change in IDO activity in the studied tissues.
Page(s): 156-159</description>
      <pubDate>Tue, 01 Apr 2014 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/28694</guid>
      <dc:date>2014-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>&lt;span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB"&gt;A novel pullulanase from a fungus &lt;i style="mso-bidi-font-style:normal"&gt;Hypocrea jecorina&lt;/i&gt; QM9414: production and biochemical characterization&lt;/span&gt;</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/28693</link>
      <description>Title: &lt;span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB"&gt;A novel pullulanase from a fungus &lt;i style="mso-bidi-font-style:normal"&gt;Hypocrea jecorina&lt;/i&gt; QM9414: production and biochemical characterization&lt;/span&gt;
Authors: Orhan, Nurdagul; Kiymaz, Nilay Altas; Peksel, Aysegul
Abstract: Pullulanase&#xD;
production from a fungus &lt;i&gt;Hypocrea jecorina&lt;/i&gt; QM9414 that produces native&#xD;
extracellular hydrolases having industrial applications was carried out in a&#xD;
shaking flask culture containing 0.5% amylopectin at a pH of 6.50 at 30&lt;span style="font-family:Symbol;mso-ascii-font-family:" times="" new="" roman";="" mso-hansi-font-family:"times="" roman";mso-char-type:symbol;mso-symbol-font-family:="" symbol"="" lang="EN-GB"&gt;°C. &#xD;
The enzyme was purified 11-fold by ammonium sulfate fractionation,&#xD;
anion-exchange and gel-filtration chromatographies with a yield of 10.12% and a&#xD;
specific activity of 1.36 &lt;span style="font-family:Symbol;&#xD;
mso-ascii-font-family:" times="" new="" roman";mso-hansi-font-family:"times="" roman";="" mso-char-type:symbol;mso-symbol-font-family:symbol"="" lang="EN-GB"&gt;± 0.14&#xD;
U/mg protein. The molecular mass of pullulanase was estimated to be 130.56 kDa&#xD;
by PAGE and SDS-PAGE, indicating that the native enzyme was a monomer. The&#xD;
optimum pH and temperature for purified enzyme was 6.5 and between 35°-65&lt;span style="font-family:Symbol;mso-ascii-font-family:" times="" new="" roman";="" mso-hansi-font-family:"times="" roman";mso-char-type:symbol;mso-symbol-font-family:="" symbol"="" lang="EN-GB"&gt;°C, respectively. The &lt;i style="mso-bidi-font-style:normal"&gt;K&lt;/i&gt;&lt;sub&gt;m&lt;/sub&gt;&#xD;
values for &lt;span style="mso-bidi-font-style:italic"&gt;amylopectin, starch and&#xD;
pullulan as substrates were 10.7, 15.5&#xD;
and 38.4 mg/mL&lt;span style="mso-bidi-font-style:italic"&gt;, respectively. The &lt;i&gt;V&lt;/i&gt;&lt;sub&gt;max&lt;/sub&gt;&#xD;
values were found to be 3.32, 3.32 and 3.82 ΔA/min &lt;span style="mso-bidi-font-style:italic"&gt;for amylopectin, starch and pullulan, respectively.&#xD;
The enzyme was stable at 40-70&lt;span style="font-family:Symbol;&#xD;
mso-ascii-font-family:" times="" new="" roman";mso-hansi-font-family:"times="" roman";="" mso-char-type:symbol;mso-symbol-font-family:symbol"="" lang="EN-GB"&gt;°C for 30&#xD;
min, but lost about 33% of its activity at 80&lt;span style="font-family:Symbol;mso-ascii-font-family:" times="" new="" roman";mso-hansi-font-family:="" "times="" roman";mso-char-type:symbol;mso-symbol-font-family:symbol"="" lang="EN-GB"&gt;°C and about 43% of activity at 90&lt;span style="font-family:Symbol;mso-ascii-font-family:" times="" new="" roman";mso-hansi-font-family:="" "times="" roman";mso-char-type:symbol;mso-symbol-font-family:symbol"="" lang="EN-GB"&gt;°C and 100&lt;span style="font-family:Symbol;&#xD;
mso-ascii-font-family:" times="" new="" roman";mso-hansi-font-family:"times="" roman";="" mso-char-type:symbol;mso-symbol-font-family:symbol"="" lang="EN-GB"&gt;°C for the&#xD;
same incubation period. Pullulanase activity was stimulated by CoCl&lt;sub&gt;2&lt;/sub&gt;,&#xD;
NiCl&lt;sub&gt;2&lt;/sub&gt;, KI, NaCl, MgCl&lt;sub&gt;2&lt;/sub&gt;, and LiSO&lt;sub&gt;4&lt;/sub&gt;. The enzyme&#xD;
was slightly inhibited by urea, CaCl&lt;sub&gt;2&lt;/sub&gt; and &#xD;
&lt;span style="font-family:Symbol;mso-ascii-font-family:" times="" new="" roman";="" mso-hansi-font-family:"times="" roman";mso-char-type:symbol;mso-symbol-font-family:="" symbol"="" lang="EN-GB"&gt;b-mercaptoethanol. The enyzmatic characteristics, substrate specificity&#xD;
and the products of hydrolysis indicated that the enzyme was similar to those&#xD;
of type II pullulanases.&#xD;
&#xD;
&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;
Page(s): 149-155</description>
      <pubDate>Tue, 01 Apr 2014 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/28693</guid>
      <dc:date>2014-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>&lt;span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:JA;mso-bidi-language:HI" lang="EN-GB"&gt;Purification of a novel chitin-binding lectin with antimicrobial and antibiofilm activities from a Bangladeshi cultivar of potato (&lt;i&gt;Solanum tuberosum&lt;/i&gt;)&lt;/span&gt;</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/28692</link>
      <description>Title: &lt;span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:JA;mso-bidi-language:HI" lang="EN-GB"&gt;Purification of a novel chitin-binding lectin with antimicrobial and antibiofilm activities from a Bangladeshi cultivar of potato (&lt;i&gt;Solanum tuberosum&lt;/i&gt;)&lt;/span&gt;
Authors: Hasan, Imtiaj; Ozeki, Yasuhiro; Kabir, Syed Rashel
Abstract: A new chitin-binding lectin was purified from &lt;span style="mso-bidi-font-style:&#xD;
italic"&gt;a Bangladeshi cultivar ‘Deshi’ of potato (&lt;i style="mso-bidi-font-style:&#xD;
normal"&gt;Solanum tuberosum&lt;/i&gt;&lt;span style="mso-bidi-font-style:italic"&gt; L.) through&#xD;
anion-exchange and affinity chromatographies using a chitin column. Sodium dodecyl&#xD;
sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular&#xD;
mass of the lectin as 20,000 Daltons.&#xD;
This molecular mass was almost half of the molecular masses of chitin-binding&#xD;
lectins derived from other potatoes. The lectin showed both bactericidal and&#xD;
growth-inhibiting activities against Gram-positive (&lt;i&gt;&lt;span style="mso-bidi-font-weight:bold" lang="EN-GB"&gt;Listeria monocytogenes&lt;/span&gt;&lt;/i&gt;) and Gram-negative (&lt;i style="mso-bidi-font-style:normal"&gt;Escherichia coli&lt;/i&gt;&lt;span style="mso-bidi-font-weight:bold" lang="EN-GB"&gt;, &lt;i style="mso-bidi-font-style:&#xD;
normal"&gt;Salmonella enteritidis&lt;/i&gt;&lt;span style="mso-ansi-language:&#xD;
EN;mso-fareast-language:JA" lang="EN-GB"&gt; &lt;span style="mso-bidi-font-weight:&#xD;
bold" lang="EN-GB"&gt;and &lt;i&gt;Shigella boydii&lt;/i&gt;&lt;span style="mso-fareast-language:&#xD;
JA;mso-bidi-font-weight:bold;mso-bidi-font-style:italic" lang="EN-GB"&gt;) pathogenic bacteria.&#xD;
It also showed antifungal activity against &lt;i style="mso-bidi-font-style:&#xD;
normal"&gt;&lt;span style="mso-bidi-font-weight:bold" lang="EN-GB"&gt;Rhizopus &lt;/span&gt;&lt;/i&gt;&lt;span style="color:black;mso-bidi-font-style:italic" lang="EN-GB"&gt;sp&lt;span style="color:black;mso-fareast-language:JA;mso-bidi-font-style:italic" lang="EN-GB"&gt;p.&lt;span style="mso-fareast-language:JA;mso-bidi-font-weight:bold;mso-bidi-font-style:&#xD;
italic" lang="EN-GB"&gt;,&lt;span style="mso-bidi-font-weight:bold" lang="EN-GB"&gt; &lt;i style="mso-bidi-font-style:normal"&gt;Penicillium &lt;/i&gt;&lt;span style="color:black;mso-bidi-font-style:italic" lang="EN-GB"&gt;sp&lt;span style="color:black;mso-fareast-language:JA;mso-bidi-font-style:italic" lang="EN-GB"&gt;p.&lt;span style="mso-bidi-font-weight:bold" lang="EN-GB"&gt; and&lt;i&gt; Aspergillus niger.&lt;/i&gt; &lt;span style="mso-bidi-font-weight:bold"&gt;Biofilm&#xD;
produced by the bacterium &lt;i style="mso-bidi-font-style:normal"&gt;Pseudomonas aeruginosa&lt;/i&gt; was dose-dependently reduced by 5-20% in 24 h after administration of the&#xD;
lectin, which was attributed to the glycan-binding property of the lectin&#xD;
having affinity to GlcNAc polymers. It was the first observation that any&#xD;
potato lectin prevented biofilm formation by &#xD;
&lt;i style="mso-bidi-font-style:normal"&gt;P. aeruginosa&lt;/i&gt; and, therefore, could have possible&#xD;
applications in clinical microbiology and biomedical science.&#xD;
&#xD;
&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;
Page(s): 142-148</description>
      <pubDate>Tue, 01 Apr 2014 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/28692</guid>
      <dc:date>2014-04-01T00:00:00Z</dc:date>
    </item>
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