Reoxidation of reduced hen egg white lysozyme fragment 1–123
| Autor: | A Vizet, Schnek Ag, José Leonis, Deconinck M, Depreter J, Perraudin Jp, Yvan Looze |
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| Rok vydání: | 1978 |
| Předmět: |
Ovalbumin
Protein Conformation Structure-Activity Relationship Cellular and Molecular Neuroscience chemistry.chemical_compound Protein structure Animals Structure–activity relationship Disulfides Molecular Biology Pharmacology chemistry.chemical_classification Disulfide bond Cell Biology Amino acid White (mutation) Enzyme Biochemistry chemistry Molecular Medicine Female Muramidase Lysozyme Chickens Oxidation-Reduction Cysteine |
| Zdroj: | Experientia. 34:1017-1018 |
| ISSN: | 1420-9071 0014-4754 |
| DOI: | 10.1007/bf01915319 |
| Popis: | The reactivation of reduced lysozyme, whose 6 COOH-terminal amino acid including cysteine 127 were cut off, was studied. The results show that the disulfide bridge I-VIII as well as the COOH-terminal hexapeptide do not play a decisive role in the acquisition of the native 3-dimensional structure of the enzyme. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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