http://nopr.niscair.res.in/handle/123456789/3690 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/3760 Title: Analysis of free nucleotide pools of mouse liver tissue by high-pressure liquid chromatography (HPLC) <br/> <br/>Authors: Abadi, Reza Haji Hosseini Baghdad <br/> <br/>Abstract: In this paper, analysis of free nucleotides from mouse liver tis-sue during different day times has been described. Perchloric acid extract of mouse liver tissue was neutralized with tri-N-octylamine in trichlorotriflouroethane and after removal of ClO^-₄, subjected to preliminary purification on a Cu²⁺-loaded column of Chelex 100. A high-pressure liquid chromatographic (HPLC) anion-exchange procedure used in the study gave a good resolu-tion of free nucleotides on a single column. <br/> <br/>Page(s): 209-212 Thu, 29 May 2003 22:58:59 GMT http://nopr.niscair.res.in/handle/123456789/3759 Title: QSAR of peripheral benzodiazepine receptor ligand 2-phenylimidazo- [1,2-a]pyridine derivatives with physico-chemical parameters <br/> <br/>Authors: Roy, Kunal; De, A U; Sengupta, Chandana <br/> <br/>Abstract: QSAR of the binding affinities of [2-phenylimidazo[1,2-a]pyridin-3-yl]acetamide derivatives (Fig. 1) with central and peripheral (from cortex and ovary) benzodiazepine receptors has been explored using physico-chemical parameters. Attempt has been made to explore the structural and/or physico-chemical requirements of the compounds that are responsible for the selective action against peripheral benzodiazepine receptors over central ones. The results indicate that the presence of bi-substitution on the carboxamido nitrogen, presence of substitutions at X and Y positions, especially, chloro substitution at X position, and presence of chloro substitution at Z position in presence of lipophilic X and/or Y substitutions increase selectivity for binding affinity with peripheral benzodiazepine receptors over central ones. <br/> <br/>Page(s): 203-208 Thu, 29 May 2003 22:58:59 GMT http://nopr.niscair.res.in/handle/123456789/3758 Title: Dipole moment in TIM ⍺/β fold proteins <br/> <br/>Authors: Vasanthi, G; Krishnaswamy, S <br/> <br/>Abstract: TIM proteins of ⍺/β barrel fold from ⍺/β class as given in SCOP database were taken for dipole moment analysis. In all, 32 structures were analyzed for their dipole moment contributions. Representative structures from 20 super families in the ⍺/β fold, with different enzyme functions and 12 protein domains of TIM family in TIM super family were considered. The active sites of these proteins are located on the C-terminal side of the β-strands. The molecules of same ⍺/β fold, but differing in their functionality also showed a common electrostatic field pattern along the barrel axis and had the dipole moment along the barrel axis and towards C-terminal end of the b-strands. However, it is observed from our calculations that the dipole moment direction is possibly a consequence of the structural fold, with distribution of charges playing a modulatory role, and does not contribute to the location of active site. We show here that apart from the commonly held view as proposed by Hol et al [Hol W G L, van Duijnen P T and Berendsen H J C (1978) Nature (London), 273, 443-446] of the role of the β helical dipole moment, the β-sheets in the barrel can also have a considerable dipole moment contribution. Taken together with our dipole moment analysis on integral membrane proteins [Vasanthi G and Krishnaswamy S (2002) Indian J Biochem Biophys 39, 93-100], this suggests the need to examine the role of dipole moment in the case of especially β sheets forming barrels. <br/> <br/>Page(s): 194-202 Thu, 29 May 2003 22:58:59 GMT http://nopr.niscair.res.in/handle/123456789/3757 Title: Characterization of goat plasma vitronectin <br/> <br/>Authors: Suchitra, S; Ashok, Vasili; Gupta, Tapas; Joshi, Paritosh <br/> <br/>Abstract: Vitronectin (VN) was isolated and characterized from goat plasma in native and denatured state. Native VN consisted of 160 and >250 kDa polypeptides, whereas denatured VN showed bands of 81 and >250 kDa on SDS-gel. Storage of 81 kDa polypeptide for 3 days at 4ºC resulted in formation of 160 and >250 kDa proteins. Hence high molecular weight forms of VN may be dimer and multimeric forms of 81 kDa monomer. Both native as well as denatured VN showed cell adhesive activity. Cells bound to native VN were round, whereas cells adhered to denatured VN were fully spread, a characteristic also observed with 81 kDa polypeptide. The 81 kDa VN bound to Heparin, whereas the 160 kDa preparation did not bind to Heparin in presence of urea. Absence of EDTA resulted in the degradation of goat VN. Similarly, addition of excess Ca²⁺ caused total degradation of VN polypeptides in buffers with EDTA, suggesting metalloprotease activity in the protein. <br/> <br/>Page(s): 186-193 Thu, 29 May 2003 22:58:59 GMT