We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Purification of argininosuccinase from Neurospora and comparison of some properties of the wild-type enzyme and an enzyme formed by inter-allelic complementation.
- Authors
Cohen, Brian B.; Bishop, John O.
- Abstract
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.
- Publication
Genetics Research, 1966, Vol 8, Issue 2, p243
- ISSN
0016-6723
- Publication type
Article
- DOI
10.1017/S0016672300010090