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Parasitol Res ; 83(5): 518-21, 1997.
Article in English | MEDLINE | ID: mdl-9197404

ABSTRACT

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. Fatty-acid binding by the protein from A. suum reproductive tissue was investigated using the Lipidex 1000 assay, which revealed the presence of a single class of fatty-acid-binding sites with an apparent dissociation constant for palmitate of about 0.8 microM.


Subject(s)
Ascaris suum/chemistry , Carrier Proteins/chemistry , Helminth Proteins/chemistry , Myelin P2 Protein/chemistry , Neoplasm Proteins , Allergens/chemistry , Amino Acid Sequence , Animals , Antigens, Plant , Brugia malayi/chemistry , Carrier Proteins/isolation & purification , Carrier Proteins/metabolism , Dirofilaria immitis/chemistry , Fatty Acid-Binding Proteins , Helminth Proteins/isolation & purification , Helminth Proteins/metabolism , Molecular Sequence Data , Myelin P2 Protein/isolation & purification , Myelin P2 Protein/metabolism , Organophosphorus Compounds , Reproduction , Sequence Homology, Amino Acid
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