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    <title>NISCAIR Online Periodicals Repository Collection: IJBB Vol.38(4) [August 2001]</title>
    <link>http://nopr.niscair.res.in/handle/123456789/15077</link>
    <description />
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        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/15308" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/15307" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/15306" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/15305" />
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    <title>The Collection's search engine</title>
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  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/15308">
    <title>Multiple isoforms of protein kinase C in lymphocytes and airway smooth muscle of guinea pig</title>
    <link>http://nopr.niscair.res.in/handle/123456789/15308</link>
    <description>Title: Multiple isoforms of protein kinase C in lymphocytes and airway smooth muscle of guinea pig
&lt;br/&gt;
&lt;br/&gt;Authors: Fatma, Sumbul; Mushinski, J Frederic; Bansal, Surendra Kumar
&lt;br/&gt;
&lt;br/&gt;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;
 
&lt;br/&gt;
&lt;br/&gt;Page(s): 280-284</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/15307">
    <title>Determination of antidiabetic activity in &lt;i&gt;Allium cepa &lt;/i&gt;(onion) tissue cultures</title>
    <link>http://nopr.niscair.res.in/handle/123456789/15307</link>
    <description>Title: Determination of antidiabetic activity in &lt;i&gt;Allium cepa &lt;/i&gt;(onion) tissue cultures
&lt;br/&gt;
&lt;br/&gt;Authors: Kelkar, S M; Kaklij, G S; Bapat, V A
&lt;br/&gt;
&lt;br/&gt;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.
&lt;br/&gt;
&lt;br/&gt;Page(s): 277-279</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/15306">
    <title>Purification of tryptic peptides for mass spectrometry using polyvinylidene fluoride Membrane</title>
    <link>http://nopr.niscair.res.in/handle/123456789/15306</link>
    <description>Title: Purification of tryptic peptides for mass spectrometry using polyvinylidene fluoride Membrane
&lt;br/&gt;
&lt;br/&gt;Authors: Kurien, B T; Matsumoto, H; Scofield, R H
&lt;br/&gt;
&lt;br/&gt;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;
&lt;br/&gt;
&lt;br/&gt;Page(s): 274-276</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/15305">
    <title>Effect of aflatoxin B1 on phosphoinositide signal transduction pathway during regeneration of liver cells following partial hepatectomy</title>
    <link>http://nopr.niscair.res.in/handle/123456789/15305</link>
    <description>Title: Effect of aflatoxin B1 on phosphoinositide signal transduction pathway during regeneration of liver cells following partial hepatectomy
&lt;br/&gt;
&lt;br/&gt;Authors: Mistry, K J; Krishna, M; Bhattacharya, R K
&lt;br/&gt;
&lt;br/&gt;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.
&lt;br/&gt;
&lt;br/&gt;Page(s): 270-273</description>
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