[A comparative intradermal test using intestinal extracts and serum of pigeons, chickens and budgerigars in patients with exogenous allergic alveolitis and in control persons]. / Vergleichende Intrakutantestung mit Intestinalextrakten und Serum von Taube, Huhn und Wellensittich bei Patienten mit exogen allergischer Alveolitis und bei Kontrollpersonen.

To compare two different sources of bird-antigens (intestinal extracts versus serum dilutions) we performed intracutaneous tests in 79 birdkeepers (34 pigeon-, 20 hen- and 25 budgerigar-keepers) and in nonexposed control persons. The bird-exposed persons were divided into 3 groups: 1. Seropositive patients with extrinsic allergic alveolitis (EAA), 2. seropositive persons without any signs of EAA (sensitized asymptomatics), and 3. exposed seronegative healthy persons. The results of the investigation demonstrate that the early skin-reaction (20 minutes after antigen-application) is nonspecific and do not have any diagnostic value. Most of patients with EAA (65.7%) and 29.6% of sensitized asymptomatics developed a positive 6-hour-(Arthus-) reaction with intestinal extracts, whereas in control groups we have not seen any Arthus reaction. Consequently, we recommend the use of intestinal extracts in the diagnostic procedure of EAA.

[Characterization of antigenic components (major and minor antigens) in an intestinal extract from pigeons]. / Charakterisierung antigener Komponenten (Major- und Minorantigene) im Taubendarmextrakt.

It is generally accepted that there is a need for standardized antigens in the diagnostic of exogenous allergic alveolitis. For this reason, ten antigens in a pigeon intestinal extract were classified in major, minor and intermediate antigens according to the distribution of specific antibodies in sera of asymptomatic and ill persons by use of crossed immunoelectrophoresis. Using a reference antiserum with antibodies against all ten detected antigens it is possible to prove a reproducible antigen composition in following preparations.

[The analysis of localization and function of proteins in eukaryotic ribosomes by means of antibodies (author's transl)]. / Analyse der Lokalisation und Funktion der Proteine von Eukaryontenribosomen mit Hilfe von Antikörpern.

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.

Localization of proteins S1, S2, S16 and S23 on the surface of small subunits of rat liver ribosomes by immune electron microscopy.

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.

Studies on proteins of animal ribosomes. XXVIII. Preparation and antigenic properties of 40 S subunit proteins of rat liver ribosomes.

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.

Localization of ribosomal protein S2 in rat liver ribosomes by immune electron microscopy.

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.