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Solid-state Photodegradation of Bovine Somatotropin (Bovine Growth Hormone): Evidence for Tryptophan-mediated Photooxidation of Disulfide Bonds by Brian L. Miller; Michael J. Hageman; Thomas J. Thamann; Lorena B. Barròn; Christian Schöneich is a Chemistry article available to read on EtoBox.
What is Solid-state Photodegradation of Bovine Somatotropin (Bovine Growth Hormone): Evidence for Tryptophan-mediated Photooxidation of Disulfide Bonds about?
Lyophilized recombinant bovine somatotropin (rbST; bovine growth hormone) is sensitive to photoinduced degradation. The underlying mechanisms of these processes are identified and presented. Lyophilized rbST was photolyzed with near-ultraviolet (UV) light between 305 and 410 nm, and the protein content was analyzed by various bioanalytical techniques, including tryptic mapping, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), amino acid analysis, and fluorescence, UV, Raman and Fourier transform infrared (FTIR) spectroscopy. The solid-state photodegradation of rbST by near-UV light exclusively targets the protein disulfide bonds. The reaction is initiated by photoionization of tryptophan (Trp) and one-electron reduction of the disulfide. However, in contrast to the behavior of other proteins in solution, rbST appears to undergo back electron transfer to restore Trp and yield a pair of cysteine (Cys) thiyL radicals, which add molecular oxygen and ultimately recombine to yield alpha-disulfoxide, thiosulfinate, and/or thiosulfonate. Photodegradation is strictly dependent on the presence of molecular oxygen, but does not involve singlet oxygen. Between 0.4 and 10%,
Who reads Solid-state Photodegradation of Bovine Somatotropin (Bovine Growth Hormone): Evidence for Tryptophan-mediated Photooxidation of Disulfide Bonds?
It is typically read by researchers, students, and practitioners in Chemistry.
- Author
- Brian L. Miller; Michael J. Hageman; Thomas J. Thamann; Lorena B. Barròn; Christian Schöneich
- Publisher
- John Wiley and Sons; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0022-3549)
- Published
- 2003
- Language
- EN
- Field
- Chemistry (Physical Sciences)