Affinity precipitation of proteins using bis-dyes.
Based on the principle of affinity precipitation of nucleotide-dependent enzymes using bis-NAD (Mosbach), Lowe et al. have recently mentioned the possibility of synthesising bis-dyes for similar applications. In this paper we report preliminary results obtained using bis-dyes in the sulphonamide form got through carbodiimide condensation of the monomer and its aminohexyl derivative for affinity precipitation. The dimer exhibited considerable selectivity for lactate dehydrogenase (90% yield). Bovine serum albumin gave a lower yield of 50% and as expected chymosin could not be precipitated by the dimer.
D000818:Animals; D002234:Carbodiimides / Q000032:analysis; D002417:Cattle; D002846:Chromatography, Affinity; D012085:Chymosin / Q000302:isolation & purification; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification; D009243:NAD / Q000031:analogs & derivatives* / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000302:isolation & purification; D013056:Spectrophotometry, Ultraviolet
D002234:Carbodiimides; D011506:Proteins; D009243:NAD; D012710:Serum Albumin, Bovine; C018812:N(2),N(2)'-adipodihydrazido-bis-(N(6)-carbonylmethyl-NAD); D007770:L-Lactate Dehydrogenase; D012085:Chymosin