Analysis of chicken bile by gel precipitation reactions using a lectin in the place of antibody

Authors
Citation
Pf. Cotter, Analysis of chicken bile by gel precipitation reactions using a lectin in the place of antibody, POULTRY SCI, 79(9), 2000, pp. 1276-1281
Citations number
25
Categorie Soggetti
Animal Sciences
Journal title
POULTRY SCIENCE
ISSN journal
00325791 → ACNP
Volume
79
Issue
9
Year of publication
2000
Pages
1276 - 1281
Database
ISI
SICI code
0032-5791(200009)79:9<1276:AOCBBG>2.0.ZU;2-G
Abstract
A lectin obtained from black turtle beans (BTB) was precipitated with IgA i n chicken bile samples in various forms of agarose gel systems. Ouchterlony -type double-diffusion (ODD) precipitation patterns between the lectin, bil e IgA, and heavy chain-specific antibody contained spurs of the type sugges tive of partial immunologic identity. The immunoelectrophoresis precipitati on patterns between the same three reactants were mirror images and fused o n the cathodic side of the immunoelectrophoresis origin. In addition to use in ODD-type gels, BTB could also be incorporated into agarose gels suitabl e for Mancini (radial immunodiffusion) or Laurell-type rocket electrophores is. Bile samples obtained from Cornell lines OS and C, broiler breeder males, a nd University of California-Davis congenic lines were investigated using BT B- and antibody-based methods. The results of this study indicated that IgA was the most frequently detected isotype in bile, occurring in 139 of 156 (89%) samples. Most bile samples (128/156; 82%) also contained IgG, whereas fewer (19/156; 12%) contained IgM. Cornell Lines appeared to differ from b roiler breeders, having a higher frequency of IgM-positive samples. Of the total bile samples studied, 11% (17/156) of samples from broiler breeders a nd the Cornell lines appeared to be devoid of IgA; the bile of one broiler breeder was found to be devoid of all three isotypes. Instances were found in which bile samples shown to be negative for IgA by antibody-ODD were sho wn to be positive by BTB-ODD. Thus BTB appears to be a suitable adjunct to antibody for the study of IgA.