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Characterization of disulfide linkages and disulfide bond scrambling in recombinant human macrophage colony stimulating factor by fast-atom bombardment mass spectrometry of enzymatic digests
| Content Provider | Semantic Scholar |
|---|---|
| Author | Glocker, Michael O. Arbogast, Brian L. Deinzer, Max L. |
| Copyright Year | 1995 |
| Abstract | Fast-atom bombardment mass spectrometry was used to study disulfide bonding patterns in heat-denatured human recombinant macrophage colony stimulating factor (rhM-CSF). The heat-denaturated protein was studied by analysis of the pattern of peptides in the proteolytic digests. Native rhM-CSF is a homodimer with intramolecular disulfide linkages between Cys7–Cys90, Cys48–Cys139, and Cys102–Cys146 and intermolecular linkages between Cys31-Cys31, and the pairs Cys157 and Cys159. Brief heating for 1 min leads to partial disulfide bond scrambling. In addition to the native disulfide bonds between Cys7–Cys90, Cys48–Cys139, and Cys31-Cys31, nonnative disulfide bonds were detected between Cys48–Cys90 and Cys48–Cys102. When heated for 5 min the disulfide bonds of rhM-CSF are completely scrambled and lead to nonnative intramolecular disulfide bonds between Cys48–Cys102 and Cys90–Cys102 and one intermolecular disulfide bond between Cys102–Cys102. |
| Starting Page | 638 |
| Ending Page | 643 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/1044-0305(95)00250-H |
| PubMed reference number | 24214390 |
| Journal | Medline |
| Volume Number | 6 |
| Alternate Webpage(s) | https://rd.springer.com/content/pdf/10.1016%2F1044-0305(95)00250-H.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/1044-0305%2895%2900250-H |
| Journal | Journal of the American Society for Mass Spectrometry |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
