Purification, characterization, and enzyme kinetics of a glutathione S transferase from larvae of the camel tick Hyalomma dromedarii.

Background: Glutathione s-transferases (GSTs) perform an essential role in detoxification of xenobiotics and endogenous compounds via their conjugation to reduce glutathione.

Results: A GST enzyme, designated tick larvae glutathione S transferase (TLGST), was purified from larvae of the camel tick Hyalomma dromedarii via ammonium sulfate precipitation, glutathione-Sepharose affinity column and Sephacryl S-300 chromatography. TLGST-specific activity was found to be 1.

Influence of probiotics on water quality in intensified Litopenaeus vannamei ponds under minimum-water exchange.

The effects of two probiotics on NH degradation, as well as the magnetic field (21.56 m tesla) on the germination and proliferation of Bacillus spores, were studied in-vitro. Additionally, the effect of these probiotics on water quality maintenance in Litopenaeus vannamei holding ponds was investigated.

Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities.

Background: Honey bee venom contains various enzymes with wide medical and pharmaceutical applications.

Results: The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee (Apis mellifera lamarckii) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE-cellulose and Sephacryl S-300 columns.

A simple and efficient purification method of native immunoreactive antigen for diagnosis of camel hydatidosis.

Background: Cystic echinococcosis (CE), a zoonotic disease that affects animal and human health, is of increasing economic importance due to high morbidity rates and high economic losses in the livestock industry.

Aim: The present study was conducted to purify the antigen from hydatid cyst fluid (HCF) with high diagnostic efficacy of camel hydatidosis using indirect enzyme-linked immunosorbent assay (ELISA).

Materials And Methods: The HCF antigen was purified using Sephacryl S-300 column chromatography.

Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii.

Apyrase is one of the essential platelet aggregation inhibitors in hematophagous arthropods due to its ability to hydrolyze ATP and ADP molecules. Here, an apyrase (TNapyrase) with antiplatelet aggregation activity was purified and characterized from the nymphs of the camel tick Hyalomma dromedarii through anion exchange and gel filtration columns. The homogeneity of TNapyrase was confirmed by native-PAGE, SDS-PAGE as well as with isoelectric focusing.