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. 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.
Timanova
A M
AM
Institute of Experimental Pathology and Parasitology, Bulgarian Academy of Sciences, Sofia.
Marti
T
T
Walter
R D
RD
Bankov
I Y
IY
D000485:Allergens / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D052179:Antigens, Plant; D017165:Ascaris suum / Q000737:chemistry*; D017178:Brugia malayi / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D004183:Dirofilaria immitis / Q000737:chemistry; D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D018996:Myelin P2 Protein / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D009363:Neoplasm Proteins; D009943:Organophosphorus Compounds; D012098:Reproduction; D017386:Sequence Homology, Amino Acid
C043517:2-(4-isothiocyanatophenoxy)-1,3,2-dioxaphosphinene 2-oxide; C093689:ABA-1 protein, Ascaris suum; D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D015801:Helminth Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D009943:Organophosphorus Compounds