Rapid purification of tonin, esterase B, antigen psi and kallikrein from rat submandibular gland by fast protein liquid chromatography.

Tonin, esterase B, antigen psi and kallikrein from the rat submandibular gland were purified by fast protein liquid chromatography with Mono P or Mono Q columns. The purity of the separated proteins was evaluated by sodium dodecyl sulphate polyacrylamide gel electrophoresis and by isoelectrofocusing in flat-bed polyacrylamide gel. Tonin and esterase B were purified by DE-52 cellulose anion-exchange chromatography and chromatofocusing on Mono P in two and three steps, respectively. Antigen psi and kallikrein were purified by a two-step procedure using DE-52 cellulose and Mono Q anion-exchange chromatography. The high resolution power of Mono Q revealed the different isoenzymes of kallikrein.