Abstract
A simple procedure for the purification of the serine protease tonin from rat submandibular glands was developed. The method involves steps of ammonium sulfate precipitation (50–80%) and gel filtration on Sephadex G-100 before complete purification by chromatofocusing on Polybuffer exchanger PBE 94 with a pH 7.4–5.0 gradient. Tonin eluted with high resolution at its isoelectric point of 6.2. After separation of Polybuffer 74 on a Bio-Gel column, the final product ran as a single M r 31,500 band on sodium dodecyl sulfate gel electrophoresis. Digestion with Staphylococcus aureus VA protease yielded peptides of M r 16,700, 10,000, and 9000. Pure tonin was used to produce affinity-purified antitonin having a binding capacity of 11 ng/μl.
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