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  <title>NOPR Collection:</title>
  <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/15077" />
  <subtitle />
  <id>http://nopr.niscpr.res.in/handle/123456789/15077</id>
  <updated>2026-10-09T18:33:53Z</updated>
  <dc:date>2026-10-09T18:33:53Z</dc:date>
  <entry>
    <title>Multiple isoforms of protein kinase C in lymphocytes and airway smooth muscle of guinea pig</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/15308" />
    <author>
      <name>Fatma, Sumbul</name>
    </author>
    <author>
      <name>Mushinski, J Frederic</name>
    </author>
    <author>
      <name>Bansal, Surendra Kumar</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/15308</id>
    <updated>2013-01-02T16:33:00Z</updated>
    <published>2001-08-01T00:00:00Z</published>
    <summary type="text">Title: Multiple isoforms of protein kinase C in lymphocytes and airway smooth muscle of guinea pig
Authors: Fatma, Sumbul; Mushinski, J Frederic; Bansal, Surendra Kumar
Abstract: The isoenzyme pattern of protein kinase C (PKC) in lymphocytes and&#xD;
airway smooth muscles (ASM) was examined by Wes tern blot using commercially&#xD;
available monoclonal&#xD;
&#xD;
antibodies. The results showed the presence of PKC α, β, γ, ε, η, μ and&#xD;
ζ  in lymphocytes and PKC α,  γ, ε, η and ζ in ASM. The unexpected feature&#xD;
was the presence of PKC γ in both lymphocytes and ASM of guinea pigs.&#xD;
Expression of this PKC isoform is usually restricted to tissues in the central&#xD;
nervous system or spinal cord. Expression of PKC δ, θ, λ and τ was not detected&#xD;
in either lymphocytes or ASM.&#xD;
&#xD;
 
Page(s): 280-284</summary>
    <dc:date>2001-08-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Determination of antidiabetic activity in &lt;i&gt;Allium cepa &lt;/i&gt;(onion) tissue cultures</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/15307" />
    <author>
      <name>Kelkar, S M</name>
    </author>
    <author>
      <name>Kaklij, G S</name>
    </author>
    <author>
      <name>Bapat, V A</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/15307</id>
    <updated>2012-12-28T16:32:27Z</updated>
    <published>2001-08-01T00:00:00Z</published>
    <summary type="text">Title: Determination of antidiabetic activity in &lt;i&gt;Allium cepa &lt;/i&gt;(onion) tissue cultures
Authors: Kelkar, S M; Kaklij, G S; Bapat, V A
Abstract: Seedling, seedling parts&#xD;
and callus cultures of onion&#xD;
were tested for&#xD;
their antidiabetic activity&#xD;
by feeding the tissue-extracts to diabetic&#xD;
rats. The results indicated much higher antidiabetic activity in callus&#xD;
cultures as compared to natural bulbs of onion. These results may be of pharmaceutical&#xD;
significance since&#xD;
the callus can be&#xD;
used as an alternative source for the isolation of&amp;nbsp; antidiabetic&#xD;
compounds.
Page(s): 277-279</summary>
    <dc:date>2001-08-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Purification of tryptic peptides for mass spectrometry using polyvinylidene fluoride Membrane</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/15306" />
    <author>
      <name>Kurien, B T</name>
    </author>
    <author>
      <name>Matsumoto, H</name>
    </author>
    <author>
      <name>Scofield, R H</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/15306</id>
    <updated>2012-12-26T16:32:49Z</updated>
    <published>2001-08-01T00:00:00Z</published>
    <summary type="text">Title: Purification of tryptic peptides for mass spectrometry using polyvinylidene fluoride Membrane
Authors: Kurien, B T; Matsumoto, H; Scofield, R H
Abstract: &lt;span style="font-size:14.0pt;font-family:&#xD;
" times="" new="" roman";mso-fareast-font-family:"times="" roman";mso-ansi-language:="" en-in;mso-fareast-language:en-in;mso-bidi-language:ar-sa"="" lang="EN-IN"&gt;A simple procedure&#xD;
for the purification of tryptic peptides, prior to mass spectrometric analysis,&#xD;
using polyvinylidene fluoride membrane (PVDF) is described. The sensitivity of&#xD;
mass spectrometric analysis is such that minor impurities in tryptic peptide digests&#xD;
suppress the signal obtained. However, we obtained useful signal, from a sample&#xD;
that did not yield any spectra earlier, by purifying the sample using PVDF&#xD;
membrane. For this. the tryptic peptide digest was first spotted on the membrane&#xD;
which was then air-dried and washed. Further, the membrane was extracted with&#xD;
trifluoroacetic acid (TFA) and acetonitrile and subjected to mass spectrometric&#xD;
analysis. This procedure enabled us to identify a cross-reactive D1 antigen on&#xD;
the neutrophil surface that bound antibodies that targeted 60 kD Ro autoantigen&#xD;
in systemic lupus erythematosus, an autoimmune disorder.&lt;/span&gt;
Page(s): 274-276</summary>
    <dc:date>2001-08-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Effect of aflatoxin B1 on phosphoinositide signal transduction pathway during regeneration of liver cells following partial hepatectomy</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/15305" />
    <author>
      <name>Mistry, K J</name>
    </author>
    <author>
      <name>Krishna, M</name>
    </author>
    <author>
      <name>Bhattacharya, R K</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/15305</id>
    <updated>2012-12-30T16:32:08Z</updated>
    <published>2001-08-01T00:00:00Z</published>
    <summary type="text">Title: Effect of aflatoxin B1 on phosphoinositide signal transduction pathway during regeneration of liver cells following partial hepatectomy
Authors: Mistry, K J; Krishna, M; Bhattacharya, R K
Abstract: Aflatoxin B&lt;sub&gt;1&lt;/sub&gt; (AFB&lt;sub&gt;1&lt;/sub&gt;)&#xD;
when administered to partially hepatectomised rats 4 hr prior to sacrifice,&#xD;
activated signalling pathway in regenerating rat liver. The activity of&#xD;
phosphatidylinositol (PI) kinase was found decreased at 30 min but increased at&#xD;
24 hr and returned to normal at 48 hr. At 30 min. inositol-IA,5-triphosphate&#xD;
(IP&lt;sub&gt;3&lt;/sub&gt;) level increased significantly whereas diacylglycerol (DAG)&#xD;
level dropped. However, at 24 hr and 48 hr, DAG and IP&lt;sub&gt;3&lt;/sub&gt; showed the&#xD;
same trend i.e. an increase in their levels. Phosphatidylinositol-4-phosphate&#xD;
levels were found to increase at 24 hr. Protein kinase C (PKC), activity from&#xD;
the particulate fraction was significantly inhibited at 30 min, followed by&#xD;
increase in activity at 24 hr and return to normal at 48 hr. Cytosolic PKC&#xD;
showed a decrease at 24 hr and a significant increase at 48 hr. At the peak of DNA synthesis (24 hr) following partial&#xD;
hepatectomy, all these signalling steps had earlier been found to be inhibited,&#xD;
but the present study shows that aflatoxin B&lt;sub&gt;1&lt;/sub&gt; administration 4 hr&#xD;
prior to sacrifice reverses the action. Activation of PKC by aflatoxin B&lt;sub&gt;1&lt;/sub&gt;&#xD;
during regeneration of liver cells when PKC in normally inhibited, may possibly&#xD;
create conditions conducive to carcinogenesis.
Page(s): 270-273</summary>
    <dc:date>2001-08-01T00:00:00Z</dc:date>
  </entry>
</feed>

