Abstract
A procedure isolating immunoglobulins specific for common gram-negative bacterial core antigens is described. A polyclonal reagent was purified by ammonium sulfate precipitation, dialysis, and column affinity chromatography. The initial vaccinal antigen was an Ra mutant Escherichia coli O111 : B4 (strain J5). The capture antigen was lipopolysaccharide derived from an Ra mutant, Salmonella typhimurium TV119 covalently-linked to an agarose matrix. Column eluants were characterized in terms of total protein concentration, IgG concentration, and EIA titer recognizing E. coli (J5). Low protein, low IgG, high EIA reading fractions were isolated, demonstrating the utility of the described technique to purify broad spectrum cross-reactive immunoglobulin reagents.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 221-226 |
| Number of pages | 6 |
| Journal | Journal of Immunological Methods |
| Volume | 129 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 25 1990 |
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Keywords
- Affinity chromatography
- Gram-negative
- Ig
- Lipopolysaccharide
ASJC Scopus subject areas
- Biotechnology
- Immunology
Cite this
Cross-reactive affinity purification of immunoglobulin recognizing common gram-negative bacterial core antigens. / Tyler, Jeff W.; Cullor, James S; Dellinger, Jon D.
In: Journal of Immunological Methods, Vol. 129, No. 2, 25.05.1990, p. 221-226.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cross-reactive affinity purification of immunoglobulin recognizing common gram-negative bacterial core antigens
AU - Tyler, Jeff W.
AU - Cullor, James S
AU - Dellinger, Jon D.
PY - 1990/5/25
Y1 - 1990/5/25
N2 - A procedure isolating immunoglobulins specific for common gram-negative bacterial core antigens is described. A polyclonal reagent was purified by ammonium sulfate precipitation, dialysis, and column affinity chromatography. The initial vaccinal antigen was an Ra mutant Escherichia coli O111 : B4 (strain J5). The capture antigen was lipopolysaccharide derived from an Ra mutant, Salmonella typhimurium TV119 covalently-linked to an agarose matrix. Column eluants were characterized in terms of total protein concentration, IgG concentration, and EIA titer recognizing E. coli (J5). Low protein, low IgG, high EIA reading fractions were isolated, demonstrating the utility of the described technique to purify broad spectrum cross-reactive immunoglobulin reagents.
AB - A procedure isolating immunoglobulins specific for common gram-negative bacterial core antigens is described. A polyclonal reagent was purified by ammonium sulfate precipitation, dialysis, and column affinity chromatography. The initial vaccinal antigen was an Ra mutant Escherichia coli O111 : B4 (strain J5). The capture antigen was lipopolysaccharide derived from an Ra mutant, Salmonella typhimurium TV119 covalently-linked to an agarose matrix. Column eluants were characterized in terms of total protein concentration, IgG concentration, and EIA titer recognizing E. coli (J5). Low protein, low IgG, high EIA reading fractions were isolated, demonstrating the utility of the described technique to purify broad spectrum cross-reactive immunoglobulin reagents.
KW - Affinity chromatography
KW - Gram-negative
KW - Ig
KW - Lipopolysaccharide
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UR - http://www.scopus.com/inward/citedby.url?scp=0025326946&partnerID=8YFLogxK
U2 - 10.1016/0022-1759(90)90442-X
DO - 10.1016/0022-1759(90)90442-X
M3 - Article
VL - 129
SP - 221
EP - 226
JO - Journal of Immunological Methods
JF - Journal of Immunological Methods
SN - 0022-1759
IS - 2
ER -