1. The literature on the egg white proteins has been reviewed. 2. The individual egg white proteins have been isolated and the methods used described. 3. The possible origin of these proteins has been discussed. An attempt has been made to elucidate this problem by refined electrophoretic techniques. No definite conclusion could be reached with the methods available. 4. The N-terminal residues of the individual proteins were examined and the results found to be in good agreement with the literature. 5. The structure of the native ovalbumin molecule has been examined by both chemical and physical means during progressive denaturation in alcohol, urea and guanidine hydrochloride. The results of the two investigations were shown to be in agreement with one another. 6. A 'six-shaped' structure has been proposed for the configuration of the native ovalbumin molecule. 7. This structure involves the hypothesis of an intra-molecular link since there is known to be a C-terminal, but no N-terminal amino acid residue. The disulphide bridge suggested by Anfinsen and Redfield (1956) hg.B been shown to be unlikely. This link has not been identified as a chemical entity although it has been suggested that low pH enables hydrogen bond breakers to rupture the molecule more easily.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:749911 |
| Date | January 1955 |
| Creators | Steven, Frank Sinclair |
| Contributors | Tristram, George Roland |
| Publisher | University of St Andrews |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://hdl.handle.net/10023/14521 |
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