Oxidation of methionine residues in equine growth hormone by chloramine-T |
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| Institution: | 1. Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, China;2. School of Nuclear Science and Technology, Lanzhou University, Lanzhou 730000, China;3. School of Nuclear Science and Technology, University of Chinese Academy of Sciences, Beijing 100049, China;4. General Research Institute for Nonferrous Metals, Beijing 100088, China |
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| Abstract: | - 1.1. Reactivity of methionine residues towards Chloramine-T was studied in the equine growth hormone.
- 2.2. With a 20.0-fold molar excess of reagent over methionine, full oxidation of the four residues of the protein is achieved.
- 3.3. Methionine 4 is the most reactive group, followed by methionines 72 and 178—methionine 123 being the less reactive residue.
- 4.4. As judged by circular dichroism spectra and binding assays, protein conformation and binding capacity to specific receptors remains unchanged even after full oxidation of all four methionine residues.
- 5.5. Results agree with data previously obtained with bovine growth hormone.
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