Summary: A fraction which inhibited chitin synthesis was partially purified from by ammonium sulphate precipitation and gel filtration. This preparation possessed chitinase activity and hydrolysed either nascent or preformed chitin. Utilization of UDP--acetylglucos-arnine by chitin synthase was not modified in the presence of the chitinase preparation, although the chitin being synthesized was degraded mainly to -diacetylchitobiose, other larger oligosaccharides and small amounts of -acetylglucosamine. The enzyme exhibited endo- and exo-chitinase properties and was localized mainly in the cytosol fraction. Its pH optimum was 6.7 and its apparent molecular weight 20600 Dal.


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