Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4
Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-62505
- Mutant proteins (muteins) of human lnterleukin-4 (llA) were constructed by means of in vitro mutagenesis. The muteins were expressed in E. co/1, submitted to a renaturation and purification protocol and analysed for biological activity. Exchange of the cysteines at either position 46 or 99 which form one of the three disulfide bridges resulted. in a nearly co•mplete loss · of biological actiyity and an unstable protein. The exchange of tyrosine 124 also inactivated the protein, while a mutation of tyrosine 56 left some residual activity.Mutant proteins (muteins) of human lnterleukin-4 (llA) were constructed by means of in vitro mutagenesis. The muteins were expressed in E. co/1, submitted to a renaturation and purification protocol and analysed for biological activity. Exchange of the cysteines at either position 46 or 99 which form one of the three disulfide bridges resulted. in a nearly co•mplete loss · of biological actiyity and an unstable protein. The exchange of tyrosine 124 also inactivated the protein, while a mutation of tyrosine 56 left some residual activity. Exchange of the other four cysteines or of · the single tryptophane had smaller etTects.…
| Autor(en): | N. Kruse, T. Lehrnbecher, Walter Sebald |
|---|---|
| URN: | urn:nbn:de:bvb:20-opus-62505 |
| Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
| Institute der Universität: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
| Sprache der Veröffentlichung: | Englisch |
| Erscheinungsjahr: | 1991 |
| Originalveröffentlichung / Quelle: | In: FEBS Letters (1991 Jul 29) 1-2, 286, 58-60. |
| Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
| Normierte Schlagworte (GND): | Biochemie |
| Freie Schlagwort(e): | Interleukin 4 (human); Recombinant; Structure-function; ln vitro mutagenesis |
| Datum der Freischaltung: | 22.03.2012 |
| Lizenz (Deutsch): |  Deutsches Urheberrecht |