作者: D. Inbar , M. Rotman , David Givol
DOI: 10.1016/S0021-9258(18)61784-3
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摘要: Abstract Protein 315, a mouse myeloma IgA protein which binds nitrophenyl ligands, and its pepsin-produced Fab' fragment have been purified by affinity chromatography. The fragments were found to be homogeneous polyacrylamide electrophoresis isoelectric focusing, possess uniform binding constant. These readily crystallizable at low salt concentration near their point (pH 4.7). Similarly crystals can obtained of the Fab'-hapten complex. Such 1:1 molar ratio hapten (e, N-dinitrophenyl lysine) protein.