In:
European Journal of Biochemistry, Wiley, Vol. 16, No. 3 ( 1970-11), p. 537-540
Abstract:
Cysteamine oxygenase has been further purified to a degree where it appeared homogeneous in disc gel electrophoresis. The purified enzyme possesses a molecular weight of 52000 when it is treated with either 8 M urea or with 0.1 % sodium dodecyl sulfate. The molecular weight of the native undissociated enzyme was 96000 when determined by dextran gel filtration and 92000 when determined by sedimentation equilibrium in the ultracentrifuge. These results are consistent with the occurrence of two similar subunits in the molecule of eysteamine oxygenase.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1970.16.issue-3
DOI:
10.1111/j.1432-1033.1970.tb01114.x
Language:
English
Publisher:
Wiley
Publication Date:
1970
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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