http://nopr.niscair.res.in/handle/123456789/3684 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/3722 Title: Numerical solution of unsteady blood flow through an indented tube with atherosclerosis <br/> <br/>Authors: Venkateswarlu, K; Rao, J Anand <br/> <br/>Abstract: The unsteady blood flow through an indented tube with atherosclerosis in the presence of mild stenosis has been studied numerically by finite difference method. The effects of hematocrit, frequency parameter, height of stenosis, parameter determining the shape of the constriction on velocity field, volumetric flow rate, pressure gradient of the fluid in stenotic region and wall shear stress at the surface of stenosis are obtained and shown graphically. <br/> <br/>Page(s): 241-245 http://nopr.niscair.res.in/handle/123456789/3720 Title: Iron dependence and zinc inhibition of duodenal cytosolic aconitase of rat <br/> <br/>Authors: Sreedhar, Bodiga; Nair, K Madhavan <br/> <br/>Abstract: The response of duodenal cytosolic aconitase (c-aconitase) to oral repletion of graded doses of iron (Fe) during Fe-deficiency was studied in rats (WNIN strain). In addition, in vitro effect of zinc (Zn) on the enzyme activity was studied using duodenal cytosol. Iron-depleted male rats were orally repleted with either 100 or 190 or 370 μg of Fe/day (n=6, each) for 2 weeks. Fe repletion was found to increase linearly the activity of duodenal c-aconitase along with the indicators of iron status. The correlation coefficient (r) between c-aconitase and haemoglobin and mucosal ferritin was 0.6453 and 0.8441, respectively. The effects of zinc (0-40 μM) in vitro on the kinetics of c-aconitase from iron-replete stock diet fed rats (n=4) showed that Zn competitively inhibited the enzyme with a Ki (app.) of 28 μM. These observations suggest that c-aconitase is a critical target involved in the assimilation of Fe and excess dietary Zn can result in negative interactions. <br/> <br/>Page(s): 250-253 http://nopr.niscair.res.in/handle/123456789/3719 Title: Kinetic studies on thermal denaturation of C-phycocyanin <br/> <br/>Authors: Patel, Anamika; Pawar, Richa; Mishra, Sandhya; Sonawane, Shailendra; Ghosh, P K <br/> <br/>Abstract: The kinetics of thermal denaturation of a biliprotein, C-phycocyanin (C-PC) isolated from Spirulina platensis were studied at different pH values, ranging from 4.0 to 8.0. The denaturation of C-PC follows the first order kinetics and rate constant at pH 5.0 and temperature 55ºC is found to be 4.37 X 10^-5 s^-1, which increases to 5.46 X 10^-5 s^-1 at pH 7.0. The denaturation rate is much higher at 65ºC and pH 7.0 (7.96 X 10^-4), as compared to at pH 5.0 (1.46 X 10^-4). The thermal stability of C-PC is more at pH 5.0, as compared to other pH values. The observed differences in entropy values at pH 5.0, as compared to other pH values indicate a considerably close fit structure of the protein at pH 5.0, which increases the stability of native structure, even at higher temperature (65ºC). <br/> <br/>Page(s): 254-257 http://nopr.niscair.res.in/handle/123456789/3718 Title: Developmental changes in intestinal brush border enzymes of rats prenatally exposed to ethanol <br/> <br/>Authors: Bhalla, Sonali; Kaur, Kamaljit; Mahmood, Safrun; Mahmood, Akhtar <br/> <br/>Abstract: The activities of lactase, sucrase, alkaline phosphatase (AP) and ϒ-glutamyl transpeptidase (ϒ-GTP) were studied in the intestinal brush border membranes of pups born to rat mothers exposed to ethanol (1 ml of 30% ethanol daily during gestation) at different days of postnatal development. The activities of lactase (at day 4-20) and sucrase (at day 20-30) were considerably reduced in response to prenatal exposure to ethanol, while AP (at day 4-30) and ϒ-GTP activities were significantly enhanced (p<0.05) at day 4, 8, 14 and 20, but there was no significant difference by day 30 of postnatal development. The observed changes in enzyme activities were corroborated by Western blot analysis of lactase, sucrase and AP. Kinetic studies revealed a change in Vmax without affecting apparent Km of enzymes under these conditions. The present findings suggest that in utero ethanol exposure to rats is embryotoxic and affects the postnatal development of various brush border enzymes, which persist long after the ethanol was withdrawn prior to birth. <br/> <br/>Page(s): 221-226