NOPR Collection:

Identification of pregnancy-associated glycoproteins by peptide mass fingerprinting in water buffalo (Bubalus bubalis)

Fri, 01 Aug 2014 00:00:00 GMT

Title: Identification of pregnancy-associated glycoproteins by peptide mass fingerprinting in water buffalo (Bubalus bubalis) Authors: Kumar, Pradeep; Saxena, Abhishake; Singh, S K; Sharma, R K; Singh, I; Agarwal, S K Abstract: Ruminant placentas synthesize pregnancy-associated glycoproteins (PAGs) during pregnancy, which serve as biomarkers of pregnancy. The present study was conducted to verify, whether PAGs are expressed in buffalo placenta by using lectin-based affinity chromatography and peptide mass finger printing (PMF). Fetal cotyledonary tissues were collected from gravid uteri procured from slaughtered house. Proteins were extracted and subjected to wheat germ agglutinin (WGA) lectin affinity chromatography to isolate the PAGs. The isolated glycoproteins were separated by one-dimensional SDS-PAGE. PMF results of the 75 kDa protein revealed presence of two PAGs (PAG-7 and -11). The PAG-7 consisted of about 170 mass signals, of which 16 were assigned to corresponding/translated cDNA sequences of buffalo PAG-7, leading to sequence coverage of 40%. PMF result of PAG-11 showed 170 mass signals, of which 15 were assigned to buffalo PAG-11, leading to sequence coverage of 34%. In conclusion, the glycoprotein isolated from placental extract corresponding to 75 kDa band on SDS PAGE gel was a mixture of PAG-7 and -11, which may help in development of suitable diagnostics for pregnancy in buffalo. Page(s): 326-330

Anti-fatigue effects of polysaccharides extracted from Portulaca oleracea L. in mice

Fri, 01 Aug 2014 00:00:00 GMT

Title: Anti-fatigue effects of polysaccharides extracted from Portulaca oleracea L. in mice Authors: Xu, Zhongxin; Shan, Ying Abstract: Portulaca oleracea L. has been used as a food and medicinal plant for thousands of years in China. Polysaccharides extracted from P. oleracea L. (POP) are its main bioactive compound and have multiple pharmacological activities. However, anti-fatigue effects of POP have not yet been tested. This study was designed to investigate the anti-fatigue effects of POP in mice using the rotarod and forced swimming tests. The mice were randomly divided into four groups, namely normal control group, low-dose POP supplementation group, medium-dose POP supplementation group and high-dose POP supplementation group. The normal control group received distilled water and the supplementation groups received different doses of POP (75, 150 and 300 mg/kg, respectively). The POP or distilled water was administered orally and daily for 30 day. After 30 days, the rotarod and forced swimming tests were performed and then several biochemical parameters related to fatigue were determined. The data showed that POP prolonged the riding times and exhaustive swimming times of mice, decreasing blood lactic acid and serum urea nitrogen levels, as well as increasing the liver and muscle glycogen contents. These results indicated that POP had the anti-fatigue effects. Page(s): 321-325

Immobilization of cellulase on TiO₂nanoparticles by physical and covalent methods: A comparative study

Fri, 01 Aug 2014 00:00:00 GMT

Title: Immobilization of cellulase on TiO₂nanoparticles by physical and covalent methods: A comparative study Authors: Ahmad, Razi; Sardar, Meryam Abstract: Immobilization of cellulase from Aspergillus niger on TiO₂nanoparticles was studied by two different approaches — physical adsorption and covalent coupling. A. niger was selected, as it is generally non-pathogenic, is found in nature in the broad range of habitats and produces cellulase extracellulary. For covalent method, TiO₂nanoparticles were modified with aminopropyltriethoxysilane (APTS). The adsorbed and covalently immobilized enzymes showed 76% and 93% activity, respectively, as compared to the free enzyme. The catalytic efficiency V_max/K_mincreased from 0.4 to 4.0 after covalent attachment, whereas in adsorption method, it increased slightly from 0.4 to 1.2. The covalently-immobilized and adsorbed cellulase lost only 25% and 50% of their activity, respectively after 60 min of incubation at 75°C. The reusability and operational stability data also showed that covalent coupling increased the stability of the enzyme. The presence of enzyme on TiO₂ nanoparticles was confirmed by Fourier-transform infrared spectroscopy. The high-resolution transmission electron microscopy (HR-TEM) and atomic force microscopy (AFM) studies indicated aggregation of enzyme when adsorbed on TiO₂ surface and a monolayer of enzyme in covalent attachment. In conclusion, covalently attached cellulase retained good activity and thermal stability, as compared to physically adsorbed enzyme. The lower amount of enzyme activity and thermal stability in case of physically adsorbed immobilized enzyme was due to aggregation of the enzyme after adsorption on TiO₂ nanoparticles, as revealed by HR-TEM and AFM. Thus, TiO₂ nanoparticles could be suitable candidates for immobilization of cellulase for industrial applications like paper, textile, detergent and food industries. Page(s): 314-320

Molecular mechanism of interaction of mitocurcumin-1 with Akt1 and STAT3: An In silico approach

Fri, 01 Aug 2014 00:00:00 GMT

Title: Molecular mechanism of interaction of mitocurcumin-1 with Akt1 and STAT3: An In silico approach Authors: Vasagiri, Nagarjuna; Kutala, Vijay Kumar Abstract: The bioavailability of curcumin is the limiting factor for its effective use in anti-cancer therapy. Recently, we reported a novel approach to enhance the cellular uptake by conjugating curcumin with triphenyl phosphonium, named mitocurcumin-1. We found that such conjugation significantly increased the uptake of curcumin in various cancer cells and caused cancer cell death by inducing apoptosis by decreasing the phosphorylation of Akt1 (Thr308) and STAT3 (Tyr705). In this study, a molecular mechanistic model deciphering the regulation of phosphorylation of Akt1 and STAT3 by mitocurcumin-1 was investigated and compared with curcumin. The protein structures were obtained from protein data bank data base and protein-ligand interaction studies were performed with mitocurcumin-1 and curcumin. Docking interaction studies of mitocurcumin-1 with Akt1 and STAT3 active sites showed a strong binding affinity of -60.4107 Kcal/mol and -51.1734 Kcal/mol respectively, suggesting mitocurcumin-1 interacted with the residues at the active sites of phosphorylation of these molecules. Further, a Chi rotationary root mean square deviation of 1.468 Å and 3.965 Å at the active sites in Akt1 and STAT3, respectively indicated that changes in the conformation of protein structure at the active site resulted in the inhibition of phosphorylation of these molecules. To conclude, by using molecular modeling approaches for the first time, we demonstrated the inhibition of Akt1 and STAT3 phosphorylation by mitocurcumin-1. Page(s): 308-313

NOPR Collection:

Identification of pregnancy-associated glycoproteins by peptide mass fingerprinting in water buffalo (Bubalus bubalis)

Anti-fatigue effects of polysaccharides extracted from Portulaca oleracea L. in mice

Immobilization of cellulase on TiO2 nanoparticles by physical and covalent methods: A comparative study

Molecular mechanism of interaction of mitocurcumin-1 with Akt1 and STAT3: An In silico approach

Immobilization of cellulase on TiO₂nanoparticles by physical and covalent methods: A comparative study