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Lipases are useful enzymes that are responsible for the hydrolysis of triacylglycerides and play an important role in plant growth. In this study, we report a rapid molecular method to amplify a partial sequence of the lipase class 3 family designated BnLIP3 gene of Brassica napus L. in order to follow its expression and analyze its role during seed germination. Therefore, we conceived PCR homologous primers to amplify the active site encoding region of the BnLIP3 family genes. Subsequently, to sequence determination of the 582 bp fragment, we deduced BnLIP3 specific primers for a nested RTPCR application. The deduced 194 amino acid sequence (Genbank 1160264) was found to share 85% of identity with lipase from Arabidopsis thaliana class 3 family. The GxSxG consensus motif near the catalytic triad at the active serine site was also identified. The peptidic sequence showed little homology with mammalian and microbial lipases. RT-PCR analysis indicated that BnLIP3 gene was expressed during B. napus seed germination.Keywords: Brassica napus L., GxSxG lipase, germination, BnLIP3, RT-PCR.African Journal of Biotechnology Vol. 12(25), pp. 3905-3913

[EN] Lipases catalyze the hydrolysis of ester bonds in triacylglycerides, generating glycerol and free fatty acids. These enzymes are encoded by extremely complex gene families, and appear to fulfil many different biological functions. Although they are present in all types of organisms, available information on plant lipases is still very limited, as compared to their bacterial and animal counterparts. A full-length clone, BnLIP, encoding a putative lipase, has been isolated by PCR amplification of Brassica napus genomic DNA, with oligonucleotide primers derived from the sequence of an Arabidopsis thaliana homologue. The clone included an open reading frame of 1581 bp encoding a polypeptide of 526 amino acids, with a calculated molecular mass of 59.5 kDa. Analysis of the deduced protein sequence, sequence alignment with homologous proteins from related plant species, and a phylogenetic analysis revealed that the BnLIP protein belongs to the classical GxSxG-motif lipase family. RTPCR assays indicated that the BnLIP gene is expressed specifically, but only transiently, during seed germination: the lipase mRNA was not present at detectable levels in ungerminated seeds, was detected only three days after seed imbibition, but its levels decreased rapidly afterwards. No expression was observed in roots, stems or leaves of adult plants. This expression pattern suggests that BnLIP is one of the lipases involved in the hydrolysis of triacylglycerides stored in rapeseed seeds, ultimately providing nutrients and energy to sustain seedling growth until photosynthesis is activated

International audience; The purpose of this study was to investigate the effect of subacute exposure to static magnetic fields (SMF) on hematological and muscle biochemical parameters in rats. Male Wistar rats, daily exposed to SMF, were exposed to SMF (128 mT, 1 h/day) during 15 consecutive days. SMF-exposed rats showed a significant decrease in red blood cell (RBC) count, hemoglobin (Hb), and hematocrit (Ht) values compared to sham-exposed rats (p

El efecto sobre el crecimiento de Salmonella hadar fue investigado utilizando un medio liquido esteril fresco (Pronadisa, Hispanlab) conteniendo el extracto acuoso de ajo (EAA) en diferentes concentraciones (0, 11, 12 y 13 mg/ml). El extracto de ajo anadido con estas concentraciones tuvo un efecto bacteriostatico sobre Salmonella hadar. La prueba serovar revelo un patron de inhibicion caracterizado por: (i) una fase de inhibicion transitoria cuya duracion fue proporcional a la concentracion de EAA, (ii) una reanudacion de la fase de crecimiento, la cual mostro una tasa mas baja de crecimiento que controles sin inhibicion, y (iii) una ingreso en fase estacionaria con una menor densidad de cultivo. La concentracion minima inhibitoria (CMI) y la concentracion minima bactericida (CMB) fueron muy cercanas, la CMI de ajo fue de 12 mg/ml y la CMB fue de 14 mg/ml. Las actividades enzimaticas seguidas con el sistema API-ZYM, mostraron cambios significativos durante la fase de inhibicion. Estos cambios bioquimicos representan una respuesta adaptativa al estres del ajo. Algunas actividades enzimaticas celulares desaparecieron, mientras que otras fueron inducidas o mantenidas despues de la adicion de EAA. Las imagenes de MET de las muestras tratadas con la concentracion del bacteriostatico EAA (12 mg/ml) revelaron la ruptura de las paredes celulares y la disposicion no homogenea de materiales citoplasmaticos dentro de las bacterias tratadas.

Background blaVEB-1 is an integron-located extended-spectrum β-lactamase gene initially detected in Escherichia coli and Pseudomonas aeruginosa strains from south-east Asia. Several recent studies have reported that VEB-1-positive strains are highly resistant to ceftazidime, cefotaxime and aztreonam antibiotics. One strategy to overcome resistance involves administering antibiotics together with β-lactamase inhibitors during the treatment of infectious diseases. During this study, four VEB-1 β-lactamase inhibitors were identified using computer-aided drug design. Methods The SWISS-MODEL tool was utilized to generate three dimensional structures of VEB-1 β-lactamase, and the 3D model VEB-1 was verified using PROCHECK, ERRAT and VERIFY 3D programs. Virtual screening was performed by docking inhibitors obtained from the ZINC Database to the active site of the VEB-1 protein using AutoDock Vina software. Results and conclusion Homology modeling studies were performed to obtain a three-dimensional structure of VEB-1 β-lactamase. The generated model was validated, and virtual screening of a large chemical ligand library with docking simulations was performed using AutoDock software with the ZINC database. On the basis of the dock-score, four molecules were subjected to ADME/TOX analysis, with ZINC4085364 emerging as the most potent inhibitor of the VEB-1 β-lactamase.