Purification of recombinant Mycobacterium leprae 65-kilodalton antigen and murine antibody responses to intravenously administered recombinant protein.
Recombinant Mycobacterium leprae 65-kilodalton antigen has been purified by a combination of differential solubility, ion-exchange and hydrophobic interaction chromatography, and a method for the quantification of the antigen in large scale protein preparations developed. By injecting large amounts of the recombinant antigen intravenously into mice, a limited degree of specific suppression of antibody-response has been induced.
Char
S
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Department of Biology, University College London, U.K.
Colston
M J
MJ
Mitchison
N A
NA
Simon
K
K
D000818:Animals; D000907:Antibodies, Bacterial / Q000096:biosynthesis*; D000942:Antigens, Bacterial / Q000008:administration & dosage / Q000276:immunology / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D003720:Densitometry; D004797:Enzyme-Linked Immunosorbent Assay; D015151:Immunoblotting; D007275:Injections, Intravenous; D051379:Mice; D008807:Mice, Inbred BALB C; D009166:Mycobacterium leprae / Q000276:immunology*; D011994:Recombinant Proteins / Q000008:administration & dosage / Q000276:immunology / Q000302:isolation & purification; D012995:Solubility
D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D011994:Recombinant Proteins