Increased eosinophil protein x levels in chronic fatigue syndrome

Chronic fatigue syndrome is a condition of unknown etiology characterized by severe fatigue and accompanied by symptoms including cognitive difficulties, myalgias, and headaches. Studies of this illness have found chronic activation of the immune system, including one reporting elevated levels of eosinophil cationic protein, considered an eosinophil activation marker. The aim of this study was to measure serum levels of eosinophil protein X, a cationic protein not measured previously in this illness. Measurements are reported on serum samples from 29 patients meeting the Centers for Disease Control and Prevention criteria for chronic fatigue syndrome, and 30 healthy controls of similar age and gender. The median serum eosinophil protein X level in patients was higher than controls: 37.9 vs. 25.3μg/L (p = 0.037). Forty-eight percent of patients versus 23% of controls had levels above the normal range. The marked increase in serum levels of eosinophil protein X in chronic fatigue syndrome patients could reflect eosinophil activation in this illness. Read More: http://informahealthcare.com/doi/abs/10.1300/J092v09n01_0

Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica

Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions