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The phenoloxidases of the ascomycetePodospora anserina: The three forms of the major laccase activity

✍ Scribed by Pascal Durrens

Publisher
Springer
Year
1981
Tongue
English
Weight
738 KB
Volume
130
Category
Article
ISSN
0302-8933

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✦ Synopsis

In Podospora anserina three laccase activities (I, II and III) were identified. Present results show the existence of an additional laccase (an anodic protein; MW 80,000; Rf 0.07). Laccase IV derived from the dissociation at acid pH (4.5) of a protein which showed identical molecular weight (390,000) and Rf (0.1) to the oligomeric laccase I. The recovery of laccase I activity when starting from ]accase IV (purified by means of isoelectric focusing) suggests that laccase I itself was the source oflaccase IV. In turn, laccase IV gave rise to the laccase III after electrophoresis or dialysis at basic pH (8.5).

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In order to learn the internal conditions for the production of the various phenoloxidases produced by the Aseomycete Podospora anserina the wild strain has been grown under controlled conditions in a fermenter for a period of 34 days. Samples were withdrawn at regular intervals and assayed for myce