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1.
Article in English | IMSEAR | ID: sea-176872

ABSTRACT

Aim: The aim of the present study was to assess the activity of Nelumbo nucifera Gaertn. Petal extract (NNPE) in tubular enzymes and in urinary albumin of Gentamicin (GM) induced renotoxic rats. Material and methods: The study was conducted for fourteen days in twenty-four rats in four groups and the study was designed as ,Group I: Control group received 0.5% CMC; Group II: GM 100mg/kg/day i.p. Group III: NNPE extract (200mg/kg/day p.o.) + GM (100mg/kg/day i.p.); Group IV: NNPE extract (400mg/kg/day p. o) + GM (100mg/kg/day i.p.).After the last injection of GM, 24-hour urine samples were collected from all the groups to analyze the levels of tubular marker enzymes N-acetyl-β-D-glusosaminidase (NAG), Gama Glutamyl transpeptidase (GGT), Alkaline phosphatase (ALP) and Lactate dehydrogenase (LDH) and Albumin in urine to determine the extent of renal tubular damage by measuring renal enzymuria and albuminuria in toxic rats induced by Gentamicin. Results: Levels of tubular marker enzymes and albumin were increased in Group-II and in treatment with N. nucifera Gaertn. Petal extract with different doses brought back to normal levels in tubular marker enzymes as well as albumin in urine for Group- III and Group- IV. Conclusions: The present study revealed that N. nucifera Gaertn. Petal extract possess potent protective effect in both doses due to its high antioxidant property against renal enzymuria and albuminuria.

2.
Indian J Exp Biol ; 2014 Feb; 52(2): 168-174
Article in English | IMSEAR | ID: sea-150346

ABSTRACT

Calcium calmodulin dependent protein ser/thr phosphatase, also referred to as protein phosphatase 2B (PP2B), is rich in neural tissue, and plays an important role in the overall function of the nervous system. Routinely phosphatase assay employs, para-Nitrophenlylphosphate (p-NPP), as a substrate, is also extended to assay PP2B. However, in the present study, the differential spectral characterstic property of tyrosine and phopshotyrosine has been exploited to employ the latter as a candidate substrate for the PP2B assay. The specific activity of PP2B using phosphortyrosine in bovine Bos Taurus indicus brain extract (Bos Taurus indicus), was measured in presence of different metal ions like Ca2+, Mn2+ and Mg2+. Further modulators like dithiothreitol (DTT), calmodulin (CaM) and metal chelators such as EGTA and EDTA were applied to confirm the role of divalent cations and to determine calcium calmodulin dependent phoshphatase activity. PP2B activity was higher with phosphotyrosine in presence of Ca2+ than with p-NPP. Further experiments, involving calmodulin as a modulator, confirmed phosphotyrosine as a better substrate over p-NPP. Calmodulin further enhanced the effect of phosphotyrosine as a potential substrate confirming calcium calmodulin dependent phosphatase activity. Phosphotyrosine is proposed as a better substrate in assaying calcium dependent phosphatase activity when compared to para-nitrophenylphosphate.


Subject(s)
Amino Acid Sequence , Animals , Brain Chemistry , Calcineurin/chemistry , Calcineurin/isolation & purification , Calcineurin/metabolism , Calcium/metabolism , Calmodulin/metabolism , Cattle , Kinetics , Phosphotyrosine/chemistry , Tissue Extracts/chemistry , Tyrosine/chemistry
3.
Article in English | IMSEAR | ID: sea-163333

ABSTRACT

Aims: To formulate and characterize GLB-PEG-LEC NCs (lecithin complexed Glibenclamide nanocrystals) and to analyze the effect of PEG 20000 and lecithin on drug properties, particle size reduction and stability of GLB NCs. Study Design: Precipitated (GLB-PEG) and complexed nanocrystals (GLB-PEG-LEC) of glibenclamide were characterized for particle size, size distribution, zeta potential and stability assessment using photon correlation spectroscopy. The crystallinity was analyzed by X-ray powder diffraction spectroscopy and differential scanning calorimetry. The chemical stability was assessed by means of infrared spectroscopy and surface morphology by scanning electron microscopy. Place and Duration of Study: Asian Institute of Medicine Science and Technology, Malaysia, between May 2102 and June 2013. Methodology: GLB-PEG NCs were prepared by precipitation technique using PEG 20000 and complexed by soybean lecithin. The effect of lecithin in particle size reduction, change in crystallinity, stability and surface properties of NCs were analyzed and compared with pure glibenclamide (GLB) and precipitated NCs. The formulations were optimized and its stability was assessed during a 3 month period. Results: Pure GLB exhibited an average particle size of 1551 nm. The average particle size of precipitated NCs was between 236 - 7000 nm, while that of complexed NCs was between 155 - 842 nm. The particle size of NC was found to decrease, whereas its zeta potential was found to increase after complexation. DSC studies showed no change in crystalline structure. PXRD studies proved that crystallinity was maintained in NCs. SEM analysis showed presence of spherical shape particles with a lipid coat on the surface after complexation. Stability studies revealed no change in particle size during 3 month period. FTIR studies showed the compatability of excipients with the drug. Conclusion: These results show that lecithin complexed GLB NCs could be utilized as promising carriers in development of various formulations due to its high stability and decreased particle size.

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