Differential phosphoproteome profiling by affinity capture and tandem matrix-assisted laser desorption/ionization mass spectrometry.

Protein phosphorylation is a ubiquitous post-translational modification that affects a significant subset of the proteome and plays an especially important role in signal transduction and cell cycle control in eukaryotic organisms. Recently developed methods that couple multidimensional liquid chromatography to electrospray mass spectrometers can be used to analyze entire phosphoproteomes. However, they require considerable investments and technical skills that are only available in a few highly specialized laboratories.

Ascaridia galli fatty acid-binding protein, a member of the nematode polyprotein allergens family.

A fatty acid-binding protein from the nematode Ascaridia galli was characterized. The gene was isolated and recombinantly expressed in Escherichia coli. According to the deduced amino acid sequence A.

Sphingomyelin synthesis in helminths: a minireview.

Sphingolipids are a diverse and ubiquitous group of lipids. They are widely distributed in parasites and a number of novel forms have been described. Sphingolipid synthesis has been investigated in the malarial parasite, cestodes, digeneans and nematodes.

Characterisation and properties of an intracellular lipid-binding protein from the tapeworm Moniezia expansa.

The tapeworm Moniezia expansa contains an extremely abundant cytoplasmic lipid-binding protein (LBP). It is a small protein consisting of 66 amino acids with a molecular mass of 7943 +/- 1.5 Da.

Isolation and partial characterization of a fatty-acid-binding protein from Ascaris suum reproductive tissue.

A 12-kDa fatty-acid-binding protein was purified to homogeneity from Ascaris suum reproductive tissue as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. N-terminal amino-acid-sequence analysis of the protein revealed its identity with the ABA-1 allergen protein isolated from A. suum pseudocoelomic fluid.