http://nopr.niscair.res.in/handle/123456789/6310 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/6986 Title: Cytosolic sulfotransferases <br/> <br/>Authors: Nimmagadda, Deepthi; Cherala, Ganesh; Ghatta, Srinivas <br/> <br/>Abstract: Sulfoconjugation (Sulfation or Sulfonation) is an important reaction in the phase II biotransformation of a wide number of endogenous and foreign chemicals, including: drugs, toxic chemicals, hormones, and neurotransmitters. The reaction is catalyzed by the members of the cytosolic sulfotransferase (SULT) superfamily, consisting of ten functional genes in humans. Sulfation reaction in living cells is reversed by sulfatase, which hydrolyses the sulfonated conjugates. It has a major role in regulating the endocrine status of an individual by modulating the activity of steroid hormones, their biosynthesis, and the metabolism of catecholamines. Sulfonation is a key reaction in the body's ‘chemical’ defense against xenobiotics. Although the primary function of sulfoconjugation is to permit detoxification of the compound, it also results in the activation of chemical procarcinogens, such as certain dietary and environmental agents into carcinogens. In this review, we summarize our current understanding of the structure of mammalian cytosolic sulfotransferases and their role in human steroid associated cancers and in the bioactivation of chemical carcinogens. <br/> <br/>Page(s): 171-182 http://nopr.niscair.res.in/handle/123456789/6976 Title: Effect of ovine follicular fluid peptide on ovarian responses and other organ weights in rats, <i style="">Rattus norvegicus Berkenhout </i>1769 <br/> <br/>Authors: Nandi, S; Kumar, V Girish; Gupta, P S P <br/> <br/>Abstract: The present study was aimed to study the effect of an ovine follicular fluid peptide on ovarian follicle and good oocyte numbers and weights of ovary, uterus, liver, pancreas and kidney in rats, <i style="">R. norvegicus</i>. A 30.1 kDa peptide was isolated from ovine follicular fluid by ammonium sulphate precipitation and then gel filtration. The peptide was tested at various levels in normal (22 and 36 day-old), superovulated (29 day-old) immature and 121-day old mature rats on the ovarian responses and other organ weights. The isolated peptide inhibited the growth of antral follicles in normal and superovulated rats. Ovarian, uterine weight and recovery of good oocytes were reduced when the peptide was administered at 100 mg dose. The peptide had no effect on kidney, liver, pancreas weight and recovery of preantral follicles. <br/> <br/>Page(s): 880-885 http://nopr.niscair.res.in/handle/123456789/6670 Title: Effect of <i style="">Aerva lanata</i> on calcium oxalate urolithiasis in rats <br/> <br/>Authors: Soundararajan, P; Mahesh, R; Ramesh, T; Begum, V Hazeena <br/> <br/>Abstract: Calcium oxalate (CaOx) stone was induced in rats using 0.75% of ethylene glycol in drinking water for 28 days. Ethylene glycol treated rats showed significant increase in the activities of oxalate synthesizing enzymes such as glycolic acid oxidase (GAO) in liver and lactate dehydrogenase (LDH) in liver and kidney. CaOx crystal deposition, as indicated by increased excretion of stone-forming constituents in urine, such as calcium, oxalate, uric acid, phosphorus and protein and decreased concentration of inhibitors, such as citrate and magnesium was observed in ethylene glycol induced urolithic rats. Histopathological studies also confirmed the deposition of CaOx crystals. Administration of <i style="">Aerva lanata</i> aqueous suspension (2g/kg body wt/dose/day for 28 days) to CaOx urolithic rats had reduced the oxalate synthesizing enzymes, diminished the markers of crystal deposition in the kidney. The results of the present study confirmed that <i style="">A. lanata</i> can be used as an curative agent for urolithiasis. <br/> <br/>Page(s): 981-986 http://nopr.niscair.res.in/handle/123456789/6669 Title: Affinity purification and partial characterization of IgM-like immunoglobulins of African catfish, <i style="">Clarias gariepinus</i> (Burchell, 1822)<b style=""></b> <br/> <br/>Authors: Rathore, Gaurav; Swaminathan, T Raja; Sood, Neeraj; Mishra, B N; Kapoor, D <br/> <br/>Abstract: IgM like macroglobulin from bovine serum albumin (BSA)-immunized African catfish <i style="">C. gariepinus</i> was purified by affinity chromatography and partially characterized. The molecular weight of this macroglobulin was 840 kDa, as estimated by gel filtration chromatography. Purified macroglobulin was analyzed using SDS-PAGE under reducing and non-reducing conditions. The molecular weight (MW) of heavy and light chain was 74.8 kDa and 27.2 kDa respectively, in presence of a reducing agent. In non-reducing SDS-PAGE, a single high MW band was observed representing tetrameric form. <br/> <br/>Page(s): 1018-1021