TY - JOUR
T1 - An antigen common to a wide range of bacteria. I. The isolation of a 'common antigen' from Pseudomonas aeruginosa
AU - Sompolinsky, D
AU - Hertz, J B
AU - Høiby, N
AU - Jensen, K
AU - Mansa, B
AU - Samra, Z
PY - 1980/6
Y1 - 1980/6
N2 - In crude water-soluble extracts of Pseudomonas aeruginosa 64 antigens can be demonstrated by crossed immunoelectrophoresis in agarose with polyvalent Pseudomonas-immunoglobulin. One of these antigens cross-reacts with antigens prepared from bacteria of a wide range of taxonomic groups. Monospecific immunoglobulins to this antigen (Common Antigen) were produced by immunization with the appropriate immunocomplex extracted from agarose. Common Antigen was purified by the combination of two fractionation methods: Precipitation of the crude extract with 18% (w/v) sodium sulfate, followed by gel filtration of the supernatant on a Sephadex G-200 column. By this method, 35% of Common Antigen from the crude extract was recovered, more than half of the fractions electrophoretically pure. Electrophoresis of reduced Common Antigen on a dodecyl sodium sulfate polyacrylamide gel revealed two protein bands with apparent molecular weights of 59-62 000 and 62-65 000, respectively. The untreated antigen, however, passed a column of Sephadex G-200 with the void volumen, indicating a substance of high molecular weight (> 4-600 000).
AB - In crude water-soluble extracts of Pseudomonas aeruginosa 64 antigens can be demonstrated by crossed immunoelectrophoresis in agarose with polyvalent Pseudomonas-immunoglobulin. One of these antigens cross-reacts with antigens prepared from bacteria of a wide range of taxonomic groups. Monospecific immunoglobulins to this antigen (Common Antigen) were produced by immunization with the appropriate immunocomplex extracted from agarose. Common Antigen was purified by the combination of two fractionation methods: Precipitation of the crude extract with 18% (w/v) sodium sulfate, followed by gel filtration of the supernatant on a Sephadex G-200 column. By this method, 35% of Common Antigen from the crude extract was recovered, more than half of the fractions electrophoretically pure. Electrophoresis of reduced Common Antigen on a dodecyl sodium sulfate polyacrylamide gel revealed two protein bands with apparent molecular weights of 59-62 000 and 62-65 000, respectively. The untreated antigen, however, passed a column of Sephadex G-200 with the void volumen, indicating a substance of high molecular weight (> 4-600 000).
KW - Antigens, Bacterial/isolation & purification
KW - Chromatography, Gel
KW - Electrophoresis, Polyacrylamide Gel/methods
KW - Epitopes
KW - Immunoelectrophoresis, Two-Dimensional/methods
KW - Pseudomonas aeruginosa/immunology
U2 - 10.1111/j.1699-0463.1980.tb02620.x
DO - 10.1111/j.1699-0463.1980.tb02620.x
M3 - Journal article
C2 - 6160723
SN - 0105-0656
VL - 88
SP - 143
EP - 149
JO - Acta pathologica et microbiologica Scandinavica. Section B, Microbiology
JF - Acta pathologica et microbiologica Scandinavica. Section B, Microbiology
IS - 3
ER -