Glutathione transferases in the tapeworm Moniezia expansa. (1/3)

Four forms of GSH transferase were resolved from Moniezia expansa cytosol by GSH-Sepharose affinity chromatography and chromatofocusing in the range pH 6-4, and the presence of isoenzymes was further suggested by analytical isoelectric focusing. The four GSH transferase forms in the cestode showed no clear biochemical relationship to any one mammalian GSH transferase family. The N-terminal of the major GSH transferase form showed sequence homology with the Mu and Alpha family GSH transferases. The major GSH transferase appeared to bind a number of commercially available anthelmintics but did not appear to conjugate the compounds with GSH. The major GSH transferase efficiently conjugated members of the trans-alk-2-enal and trans,trans-alka-2,4-dienal series, established secondary products of lipid peroxidation.  (+info)

Axenomycins, new cestocidal antibiotics. (2/3)

Axenomycins are a new group of macrolide antibiotics isolated from the fermentation broth of Streptomyces lisandri n.sp. They exhibit anthelmintic activity against tapeworms (Cestoda). Three different fractions, A, B, and D, have been obtained, the most active fraction being axenomycin D. The activities of the axenomycin complex and axenomycin D against Hymenolepis nana in mice, Taenia pisiformis, Dipylidium caninum, and Diphyllobothrium sp. in dogs, and Moniezia expansa, M. benedeni, and Avitellina centripunctata in lambs were studied in experimentally and naturally infected animals. Axenomycins were effective and well tolerated by the oral route. Worm reduction rates after a single oral dose were 90 to 100% with 5 to 10 mg of axenomycin D/kg and 50 to 100% with 20 mg of axenomycin complex/kg.  (+info)

Characterisation and properties of an intracellular lipid-binding protein from the tapeworm Moniezia expansa. (3/3)

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. The amino acid sequence has been established by Edman degradation and confirmed by PCR analysis. The Moniezia LBP shows no sequence similarity with any previously described binding protein, but does show similarity with antigen B from Echinococcus glanulosus and Echinococcus multilocularis and with Taenia crassiceps antigen. The predicted structure for Moniezia LBP shows four helices and a putative tyrosine kinase site on the loop between helix 1 and 2. Each of the four helices has a well defined hydrophobic face. Studies with fluorescent probes suggest a single hydrophobic binding site. Results indicate that the single tryptophan residue in the molecule (Trp41) is involved in ligand binding, and calculation of the Stern-Volmer quenching constant shows that Trp41 is in a relatively hydrophobic environment.  (+info)