1887

Abstract

Summary

Extracellular opacity factor (OF) from group-A M-type 22 was purified by ammonium sulphate precipitation followed byion-exchange on DE-52 cellulose and gel filtration on sephacryl S-400. OF was eluted near the void volume and shown to be heterogenous by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Antiserum to ammonium sulphate-purified OF from a cell-free culture supernate was prepared in rabbits. All preparations of OF from supernate and cell-extract were inhibited by the antiserum. No M protein was detected in the OF samples from various purification steps. The purified OF showed activity at a broad pH range with optimal activity at pH 6; it was inactivated considerably at high temperatures. Enzyme activity was inhibited by pepstatin A, but was unaffected by serine proteinase inhibitor, aprotinin, ethylene diamine trichloroacetic acid, N-ethylmaleimide, iodoacetamide and mercaptoethanol. This suggests that OF is an aspartic proteinase.

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/content/journal/jmm/10.1099/00222615-33-1-55
1990-09-01
2019-10-17
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http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-33-1-55
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