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Purification of argininosuccinase from Neurospora and comparison of some properties of the wild-type enzyme and an enzyme formed by inter-allelic complementation

Published online by Cambridge University Press:  14 April 2009

Brian B. Cohen  and
John O. Bishop
Brian B. Cohen
Affiliation:
Institute of Animal Genetics, West Mains Road, Edinburgh
John O. Bishop
Affiliation:
Institute of Animal Genetics, West Mains Road, Edinburgh

Extract

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Argininosuccinase has been purified from wild-type Neurospora crassa, strain ST.A. The purified enzyme, which is homogeneous by the criteria of analytical centrifugation and starch-gel electrophoresis, has a molecular weight of about 175,000. The enzyme has also been partially purified from a heterokaryon between the arg-10 mutant stocks B317–9–9a and 402–3a.

The reaction kinetics of the two enzymes were compared in several respects, and they were found to be indistinguishable. The enzymes were also indistinguishable by starch-gel electrophoresis, and sedimented at the same rate through a sucrose gradient. It seems likely, however, that the enzymes do differ physically since they showed different affinities for both calcium phosphate gel and hydroxylapatite during purification.

Type
Research Article
Information
Genetics Research , Volume 8 , Issue 2 , September 1966 , pp. 243 - 252
Copyright
Copyright © Cambridge University Press 1966

References

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