| Literature DB >> 7225326 |
A R Kornblihtt, M M Flawia, H N Torres.
Abstract
Testicular, soluble adenylate cyclase has been purified by anion-exchange chromatography, gel filtration, and isoelectric focusing. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peak fractions from the latter purification step showed only one polypeptide band with an apparent molecular weight of about 69 000. The following hydrodynamic and molecular parameters have been established for this enzyme: sedimentation constant, 4.3; Stokes radius, 3.95 nm; partial specific volume, 0.74 mL.g(-1); molecular weight, 74 000; fractional ratio, 1.4.Entities:
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Year: 1981 PMID: 7225326 DOI: 10.1021/bi00508a033
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162