Abstract: Process for preparing a detoxified polysaccharide-outer membrane protein complex from bacterial envelopes; the so-obtained products which are useful as vaccines against infection by the same bacteria and method for protecting animals against the same infection by administration of a pharmaceutical composition containing the detoxified polysaccharide-outer membrane protein complexes.

Abstract: A method for obtaining bacterium pili subunits directly from specified bacteria is disclosed and claimed. Dependent upon the bacterium from which the pili subunits are to be obtained, the pH of extraction solutions will be adjusted accordingly. Pili subunits obtained in accord with the method of this invention are useful for preparing vaccines which exhibit good protection against heterologous strain infections.

Abstract: There is disclosed an improved method for separating and recovering proteins, particularly therapeutically active proteins, from an aqueous system also containing a component having the ability to create two liquid phases by use of salt partitioning technology. By the addition of water soluble inorganic salts to an aqueous system containing one or more therapeutically active proteins or nucleic acids, especially an aqueous system obtained from fractionation of a blood plasma fraction or from a tissue culture fluid resulting from a biotechnology production operation such as recombinant DNA and monoclonal antibody technologies, the aqueous system may be separated into two or more liquid phases. Such separated phases may be selectively enriched in components of the original aqueous system having differing solubility in the so-separated liquid phases.

Abstract: The process is applicable to the supernatant of engineered yeast cells disrupted in the presence of a non-ionic detergent: it comprises the precipitation of contaminants by polyethylene glycol and the treatment cation or, after eventual ultrafiltration, with ammonium sulfate.

Abstract: Methods of solubilization and naturation of somatotropin protein from refractile bodies of host cells are disclosed. The solubilization methods embrace the discovery that an aqueous urea solution can be effectively used to solubilize refractile bodies containing such somatotropin protein. Surprisingly, it has been further found that once solubilized, such somatotropin protein can be natured in the urea solution by contacting the solution with a mild oxidizing agent for a time sufficient to result in the formation of the disulfide protein. Naturation can efficiently occur even at high protein concentration, in an impure preparation and in the absence of reducing agent.

Abstract: A method of preparing a solution of lactic or colostric immunoglobulins or both by processing milk or colostrum or both accompanied by precipitation of the caseins, characterized in that milk or colostrum or both are acidified to a pH of 4.0-5.5, subjected to cross-flow filtration in a filtration unit with a mean pore size of 0.1-1.2 .mu.m, and the low-molecular components removed by means of further cross-flow filtration in another filtration unit with a limit of separation of 5 000-80 000 daltons, as well as an agent for treating bacterial and viral infections that consists of a solution obtained by means of said method.

Abstract: The protein PP.sub.20 is described, this having the following characteristics:(a) an electrophoretic mobility which is somewhat larger than that of albumin,(b) an isoelectric point of 4.65.+-.0.1,(c) a sedimentation coefficient s.sub.20,w of 4.1.+-.0.1 S,(d) a molecular weight determined by electrophoresis in sodium dodecyl sulfate (SDS)-containing polyacrylamide gel of 50,000.+-.10,000, the molecules of PP.sub.20 being composed of apparently identical subunits which have a molecular weight of 27,000.+-.3,000 and are held together non-covalently,(e) an extinction coefficient E.sub.1cm.sup.1% (280 nm) of 9.5.+-.0.6,(f) a carbohydrate content of 3.0.+-.1.3%, including mannose 0.14.+-.0.05%, fucose 0.13.+-.0.05%, galactose 0.61.+-.0.2%, glucose 0.39.+-.0.2%, N-acetylglucosamine 0.95.+-.0.3%, N-acetylgalactosamine 0.18.+-.0.1%, and N-acetylneuraminic acid 0.6.+-.0.4%.(g) a specified aminoacid composition, and a process for obtaining it is described.