Properties and immunochemical reactivities of carboxy-modified human serum albumin.
Seven carboxy modified and four amino modified derivatives of human serum albumin have been prepared and studied by optical rotatory dispersion measurements, gel filtration, immunoelectrophoresis, immunodiffusion and by use of an ammonium sulphate technique. It is found that carboxy groups are of major importance for the maintenance of the structure and function of human serum albumin, and that carboxy modification has a much more profound effect than amino modification has to the same relative extent.
D000645:Ammonium Sulfate; D002850:Chromatography, Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D009905:Optical Rotatory Dispersion; D012709:Serum Albumin / Q000031:analogs & derivatives / Q000276:immunology* / Q000378:metabolism; D013329:Structure-Activity Relationship
D012709:Serum Albumin; D000645:Ammonium Sulfate