Biomedical subjects
Publications and source records attributed to F Noll.
L-type pyruvate kinase from several tissues was purified by a micro-method of immunaffinity chromatography and the subunit structure analysed by SDS-electrophoresis (1-3). Whereas in adult human kidney L as well as L' seem to be present in the normal erythrocyte only L' subunits could be identified.
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The overall shape and dimensions of IgG (rabbit) and IgY (chicken) antibodies against ribosomal proteins have been studied in electron micrographs of ribosome-antibody complexes. The antibodies appear as Y-shaped molecules with an angle of about 90 degrees between their Fab arms. The length of one Fab arm amounts to about 10 nm. No differences between the IgG and IgY molecules could be detected electron microscopically. The data obtained on the shape of IgG and IgY correlate with those of earlier electron microscopic studies while the determined size of the Fab arms is in the range found by scattering methods.
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Due to their high specificity antibodies reveal possibilities for a detailed analysis of structure and function of eukaryotic ribosomes. By means of specific antibodies against single ribosomal proteins we could (1) localize immunoelectron microscopically certain proteins at the surface of ribosomes and (2) determine their role within protein biosynthesis by the binding of the initiation factor eIF-2 to the small ribosomal subunit. The combination of the results of both methods provides evidence of the localization of the peptidyl-tRNA binding site in the head area of the small subunit of ribosomes.
Preincubation of a cell-free poly(Phe) synthesis system in the cold results in a manifold stimulation of the polyphenylalanine synthesis. This stimulatory effect can be observed only if ribosomal subunits, poly(U), Mg++ and cytosolic fraction are present in the reaction mixture during cold pretreatment. This effect is abolished if the samples are preincubated at 37 degrees C before the cold treatment probably because of an inactivation of protein factors present in the cytosolic fraction.
Ribosomal proteins S1, S2, S16 and S23 were localized on the surface of the small subunit (40S) of rat liver ribosomes by immune electron microscopy. Antibodies against the single proteins were raised in rabbits and chicken and purified by affinity chromatography. 40S-IgG-40S complexes were obtained by incubation of 40S subunits with non-cross-reacting antibodies specific for each of the four proteins and subsequent sucrose density gradient centrifugation. The location of the proteins was determined by means of antibody binding sites visualized in negative contrast in the electron microscope. The four investigated proteins are mainly located in the head region of the small subunit. Exposed antigenic determinants of proteins S1 and S2 were found to be located at different sites of the small subunit whereas proteins S16 and S23 were mapped in a limited region only.
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By combination of ion exchange chromatography, gel filtration, preparative polyacrylamide gel electrophoresis and perchloric acid fractionation 21 proteins of the small ribosomal subunit of rat liver were isolated with a purity of more than 95%. It could be demonstrated by immunological studies that no extensive structural homologies exist between these proteins.
Informatin, the protein moiety of nuclear pre-mRNA containing particles, exhibits species specific antigenic properties but shows also some interspecies cross-reactivities.
Only very small amounts of informatin could be detected in cytoplasmic polysomes with the aid of antiinformatin antibodies. This low amount of informatin cannot represent a structural component of polysomes or polysomal mRNP.
Electron micrographs of negatively stained small subunits of rat liver ribosomes have been processed by computer-assisted accumulation. The resulting micrographs are characterized by a significant noise suppression and enhancement of image details.
For small subunits of rat liver ribosomes three binding sites for antibodies specific for protein S2 have been proved: one in the head region and the two others in the neck region, suggesting that protein S2 has an elongated structure in the small subunit.
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