1887

Abstract

Summary: Autolysis of purified cell walls resulted in the release of several components thought to be mannoprotein in nature, since they were retained by Concanavalin A-Sepharose. The most abundant was a 29 kDal molecule which was also a major species among mannoproteins solubilized by the -glucanase complex Zymolyase. There was a concomitant release of glucose and mannose oligosaccharides and of -glucanase activity. Glucanase and protease inhibitory treatments considerably lowered the release of mannoproteins. The use of different protease inhibitors during autolytic incubations interfered with at least two proteases (one of them being a cysteine protease) apparently involved in the solubilization and partial degradation of mannoproteins from the walls.

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1985-11-01
2022-01-23
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