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THE NATURE OF THE MULTIPLE FORMS OF BOVINE THIOL: PROTEIN DISULFIDE OXIDOREDUCTASE
| Content Provider | Scilit |
|---|---|
| Author | Pace, Mario Dixon, Jack E. |
| Copyright Year | 2009 |
| Description | Journal: International journal of peptide and protein research Preparations of thiol"protein disulfide oxidoreductase from bovine liver were shown to be homogeneous by polyacrylamide gel electrophoresis, sedimentation equilibrium centrifugation and NH2-terminal analysis (Carmichael et al., 1977). When the enzyme was subjected to prolonged storage at -20 degrees, freeze-thawing, or heating at 60 degrees, at least one new protein species was observed using polyacrylamide gel electrophoresis. The new protein results from dimerization of the enzyme. The dmier consisted of two monomers held together by an intermolecular disulfide bond. The formation of this dimer can be reversed and partially prevented by thiols. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1399-3011.1979.tb01952.x/pdf |
| Ending Page | 413 |
| Page Count | 5 |
| Starting Page | 409 |
| ISSN | 03678377 |
| DOI | 10.1111/j.1399-3011.1979.tb01952.x |
| Journal | International journal of peptide and protein research |
| Issue Number | 5 |
| Volume Number | 14 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2009-01-12 |
| Access Restriction | Open |
| Subject Keyword | Journal: International journal of peptide and protein research Disulphide Bonds Protein Dimerization Thiol Reagents |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry |
