Pesticide residues in traditional and industrial honey marketed in Morocco and potential health risk.

This study evaluated the presence of the three pesticides methomyl (MET), carbendazim (CBZ) and chlorpyrifos-ethyl (CPE), as well as the degradation product of CPE (3,5,6-trichloro-2-pyridinol; TCP), in 44 honey samples from all 12 regions of Morocco. With a validated HPLC-UV method occurrence frequencies of 63.6% for MET, 54.

Protective Effect of Some Essential Oils Against Gamma-Radiation Damages in Tetrahymena pyriformis Exposed to Cobalt-60 Source.

The main purpose of this study was to investigate the protective effect of Rosmarinus officinalis, Origanum compactum, Lavandula angustifolia, and Eucalyptus globulus essential oils (EOs) against gamma-radiation-induced damages on Tetrahymena pyriformis growing in presence of cobalt-60 source. The chemical composition of the 4 EOs was analyzed by gas chromatography-mass spectrometry. The protective effects of EOs on growth, on morphology, and on some metabolic enzymes and antioxidant markers have been evaluated.

Changes in Growth, Morphology, and Physiology of Tetrahymena pyriformis Exposed to Continuous Cesium-137 and Cobalt-60 Gamma-Radiation.

This study investigated the effects of gamma-radiation on Tetrahymena pyriformis. The experimental approach consists of exposing T. pyriformis growing in presence of Cesium-137 (Cs) at dose rates of 1, 2, 4, and 6 cGy h and Cobalt-60 (Co) at dose rates of 8, 10, 15, and 20 cGy h.

Effects of the Cobalt-60 gamma radiation on glyceraldehyde-3-phosphate dehydrogenase.

Purpose: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of the glycolytic pathway, can play a physiological regulatory role and vital other roles in metabolism. This study investigated the effects of gamma radiation generated by Cobalt-60 source on GAPDH activity and protein levels in as an eukaryotic organism model.

Materials And Methods: After purification of the GAPDH from , in vitro effects of irradiation to the dose of 2 Gy, using Cobalt-60 at the dose rate of 0.

Silica-coated calcium pectinate formulations for controlling carbendazim release: water and soil release studies.

This study aims to encapsulate the fungicide carbendazim using a biodegradable polymer (pectin). First, we have obtained calcium pectinate beads (CPG-Carb) by ionotropic gelation using calcium ions as a crosslinking agent. These beads were then coated with silica starting from tetraethoxysilane (TEOS), by a sol-gel process to form hybrid beads (CPG-Carb-SG).

Lateral flow immunogold assay as a rapid detection tool for screening of congenital hypothyroidism.

Congenital hypothyroidism (CH) is one of the most common preventable causes of mental retardation. The majority of infants are diagnosed after detection through newborn screening programs using thyroid-stimulating hormone (TSH) test. A rapid immunochromatographic lateral flow assay based on monoclonal antibodies (MAbs) colloidal gold nanoparticles was developed in a sandwich format for the detection of TSH.

Immunoaffinity purification and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes.

A new procedure utilizing immunoaffinity column chromatography has been used for the purification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.

Effects of oxidative and nitrosative stress on Tetrahymena pyriformis glyceraldehyde-3-phosphate dehydrogenase.

Previous reports showed that hydrogen peroxide and the NO-generating reagent sodium nitroprusside (SNP)-modulated enzymatic activity of animal glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.

Cloning, gene expression and characterization of a novel bacterial NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Neisseria meningitidis strain Z2491.

Alignment of the amino acid sequence of some archaeal, bacterial and eukaryotic non-phosphorylating glyceraldehydes-3-phosphate dehydrogenases (GAPNs) and aldehyde dehydrogenases (ALDHs) with the sequence of a putative GAPN present in the genome of the Gram-negative bacterium Neisseria meningitidis strain Z2491 demonstrated the conservation of residues involved in the catalytic activity. The predicted coding sequence of the N. meningitidis gapN gene was cloned in Escherichia coli XL1-blue under the expression of an inducible promoter.

Purification and characterization of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the dromedary camel.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.

Widespread occurrence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase among gram-positive bacteria.

The non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPDHN, NADP+-specific, EC 1.2.1.

Different thermostability of skeletal muscle glyceraldehyde-3-phosphate dehydrogenase from hibernating and euthermic jerboa (Jaculus orientalis).

In previous study, we demonstrated that the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.

Purification of recombinant non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Streptococcus pyogenes expressed in E. coli.

Streprococcus pyogenes gapN was cloned and expressed by functional complementation of the Escherichia gap mutant W3CG. The IPTG-induced NADP non-phosphorylating GAPDH (GAPN) has been purified about 75.4 fold from E.

Expression, purification, and characterization of recombinant nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Clostridium acetobutylicum.

Clostridium acetobutylicum gapN was cloned and expressed in Escherichia coli BL-21. The IPTG-induced nonphosphorylating NADP-dependent GAPDH (GAPN) has been purified about 34-fold from E. coli cells and its physical and kinetic properties were investigated.

A phosphate-stimulated NAD(P)+-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of central carbon metabolism, was studied in a Bacillus cereus strain isolated from the phosphate layer from Morocco. Enzymatic assays with cell extracts demonstrated that when grown on Luria-Bertani (LB) medium, B. cereus contains a major NAD+-dependent GAPDH activity and only traces of NADP+-dependent activity, but in cells grown on Pi-supplemented LB medium a strong increase of the NADP+-dependent activity, that became predominant, occurs concurrently with a GAPDH protein increase.

Glyceraldehyde-3-phosphate dehydrogenase from the newt Pleurodeles waltl. Protein purification and characterization of a GapC gene.

The NAD(+)-dependent cytosolic glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.