Antigenic analysis of purified surface antigens of filarial nematode Setaria digitata.
The surface antigens of S. digitata were isolated by treatment with Triton X-100. In non SDS-PAGE the surface antigen preparation resolved into more than 6 protein bands. Electroelution of gel slices corresponding to the protein bands with relative mobilities 0.09, 0.32, 0.41, 0.53, 0.61 and 0.76 gave 6 purified surface antigen fractions (SAF). Analysis of SAFs by SDS-PAGE showed that the proteins with molecular weights 17, 29 and 36 KD were the three major polypeptides and different combination of these gave rise to the 6 native surface proteins. The 29 KD protein existed as a monomer and as cross-linked with the 17 and 36 KD proteins. All surface antigen fractions showed antigenicity, where as 29 KD protein remained as a high avidity surface antigen.
Bright
J J
JJ
Department of Biochemistry, University of Kerala, Thiruvananthapuram, India.
Raj
R K
RK
D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology; D000947:Antigens, Helminth / Q000276:immunology* / Q000302:isolation & purification; D000954:Antigens, Surface / Q000276:immunology* / Q000302:isolation & purification; D002417:Cattle / Q000469:parasitology; D002418:Cattle Diseases / Q000469:parasitology; D003429:Cross Reactions; D015801:Helminth Proteins / Q000276:immunology / Q000302:isolation & purification; D008970:Molecular Weight; D017182:Setaria Nematode / Q000276:immunology* / Q000302:isolation & purification; D012719:Setariasis / Q000469:parasitology
D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D000954:Antigens, Surface; D015801:Helminth Proteins