Ion-exchange high-performance liquid chromatographic studies on sulphydryl-catalysed structural alterations of bovine mercaptalbumin.
The N-A isomerization (the intramolecular SH/S-S exchange reaction) of bovine mercaptalbumin (BMA) in alkaline medium was studied by using ion-exchange high-performance liquid chromatography (HPLC) and moving-boundary electrophoresis. Results obtained by ion-exchange HPLC on the N-A isomerization of BMA were consistent with those by moving-boundary electrophoresis and showed at least two kinds of the A-form, A1 and A2, indicating that the N-A isomerization is a multi-step reaction. The rate of the N-A isomerization was strongly suppressed in [2H]water solution. The suppression by [2H]water might support the current view that intra- and intermolecular hydrophobic and/or hydrogen bonds are strengthened in [2H]water.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D007700:Kinetics; D012709:Serum Albumin / Q000032:analysis*; D012710:Serum Albumin, Bovine / Q000032:analysis*; D013438:Sulfhydryl Compounds / Q000032:analysis*; D014867:Water
D012709:Serum Albumin; D013438:Sulfhydryl Compounds; C001702:mercaptoalbumin; D014867:Water; D012710:Serum Albumin, Bovine