Magisterarbeit eingereicht an der Philosophischen Fakultät der Johann W. Goethe Universität in Frankfurt/Main, April 1984. Die Arbeit behandelt die vermeintlich dem daoistischen Meister Lü Dongbin (Tang-Dynastie) zugeschriebenen Kommentare zum Dao De Jing (Tao Te Ching, Laozi, Lao-Tzu). Diese reichen in ihrem Spektrum von philosophischen Spekulationen zu handfesten und praktischen Anweisungen alchemischer bzw. meditativer Praktiken (neidan, waidan). Sechs Kommentare wurden identifiziert und analysiert. Von jedem Kommentartext wurden die Kapitel 1, 6 und 18 übersetzt und näher betrachtet.
A system is described which permits the efficient synthesis of single proteins in vitro. The essential element in this expression system is a strong promoter derived from coliphage T5 which produces, with high efficiency, specific RNAs in capped or uncapped form, depending upon the experimental conditions used. The transcription-coupled capping of RNA allows the direct translation of the RNA in eukaryotic extracts from wheat germ as well as from HeLa cells. The synthesis of three different proteins is reported, including lysozyme, which is shown to be translocated across membranes when appropriate assay conditions are used. The simplicity of the experimental procedure, the high purity and specific activity of the [35S]methionine-labefled proteins produced offer a number of possibilities for the study of structure-function relationships of proteins.
The invariant (Ii) chain is a membrane-spanning glycoprotein found intracellularly associated with class II major histocompatibility complex (MHC) molecules. Using hybridselected translation and the Ii-specific monoclonal antibody In-1, we have isolated a cDNA clone (pli-5) coding for most of the Ii chain. Sequence analysis of this clone reveals an open reading frame encoding 169 amino acid residues. The protein is rich in methionine and contains two potential N-glycosylation sites. No stretch of uncharged amino acid residues, characteristic for a membrane-spanning segment, is found close to the COOH-terminal end. There is one, however, close to the NH2-terminal end. As it is known that -20 amino acid residues of Ii chain are exposed on the cytoplasmic side, we conclude that the Ii chain spans the membrane exposing the NH2 terminus on the cytoplasmic side and the COOH terminus on the luminal side.