Abstract: The invention concerns unique immobilized immunoglobulin-binding protein materials which have a high binding capacity for immunoglobulins. Exemplified are preparations which have a high binding capacity for IgGl immunoglobulins. The preparations are made by covalently joining an immobilization support material to (a) an arginine-containing linker and (b) an immunoglobulin-binding protein material. The immunoglobulin-binding protein can be joined to the linker through an amide bond. Specifically disclosed is an immobilized protein A preparation. This immobilized protein A preparation has utility in the art of purifying monoclonal antibodies.

Abstract: A substantially pure, hemagglutinin-free composition of trichosanthin, and a method of producing the composition is disclosed. A plant extract from Trichosanthes kirilowii is contacted with an anionic exchange resin to remove contaminating hemagglutinins, and trichosanthin is further purified from the extract by cation exchange chromatography to a purity of greater than 95%.

Abstract: Affinity-purified protein A preparations are contacted with a suitable anionic exchange material in order to remove trace contamination. Staphylococcal enterotoxin B (SEB) and other proteinaceous contaminants are removed by passing such affinity-purified protein A preparations through a DEAE-cellulose column and thereafter selectively eluting the protein A to separate the contaminants. Very high purity protein A composition are thus obtained, typically having a contaminant concentration of about 5 weight % or below, with below about 0.001 weight % SEB.

Abstract: A method of purifying PAI-1 from a biological fluid source, e.g. conditioned media of Hep G2 or HT 1080 cells, containing PAI-1 is disclosed, which comprises subjecting the biological fluid to a modified urokinase affinity absorbent, e.g. anhydrourokinase ligand bound to a CNBr-activated agarose gel or urokinase mutated at amino acid position 356 from Ser to Gly and bound to the gel, and then eluting PAI-1 from said affinity absorbent. A method of stabilizing and/or activating PAI-1 is also disclosed, which comprises complexing PAI-1 with vitronectin.

Abstract: A method is described for the purification of crude human interferon from solutions containing it, which comprises:a) the complete adsorption of the crude interferon in a column of siliceous material which has previously been disinfected with an aqueous solution of formaldehyde;b) the washing of the column with non-pyrogenic, sterile, deionized water;c) the removal of the extraneous residual proteins by the elution of the column successively with a 1.4 M aqueous solution of NaCl in non-pyrogenic, sterile, deionized water, and with an aqueous solution of acetic acid having a molar concentration of 0.001 M to 0.003 M;d) the elution of the interferon from the column with an aqueous solution of acetic acid having a molar concentration of from 0.01 to 0.03 M and finally,e) the recovery and lyophilization of the elution containing the purified interferon.

Abstract: A method for solubilization and naturation of somatotropin using an aqueous alkaline solution results in lower dimer formation and eliminates denaturants and separate renaturation steps and agents.

Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight contaminating proteins by directly adding a flocculant to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants is disclosed.The high molecular weight precipitates are removed and the solution is further processed to remove low molecular weight contaminating proteins and other non-protein contaminants. The recombinant protein is subsequently recovered and further processed to produce a protein composition suitable for its intended use.

Abstract: The invention relates to a method for the purification of the a subunit of factor XIII by affinity chromatography, to a therapeutic composition containing the latter, and to the use of the therapeutic composition.Factor XIII has hitherto been purified either by methods which are technically very elaborate or else by use of toxic affinity chromatography materials. The invention has the aim of providing an improved method for the purification of the a subunit of factor XIII.Factor XIII is obtained according to the invention by a method in which the a subunit of factor XIII is reversibly bound to a matrix suitable for disulfide exchange reactions and is removed from the matrix by reaction with a reducing agent. The method according to the invention makes it possible to provide the biologically active a subunit of factor XIII in high purity.

Abstract: This invention relates to a process for continuously fractionating plant, animal or human proteins by selective precipitation of the proteins resulting from placing a solution of proteins in contact with a precipitating agent constituted by a fatty acid of 6 to 14 carbon atoms, such as caprylic acid, is characterized in that respective deliveries of fatty acid and of the protein solution are continuously placed in contact in a mixing chamber of small volume with respect to the deliveries, creating a strong stirring in this mixing chamber; the individual deliveries of fatty acid and of protein solution are adjusted to controlled pH and temperature so as to maintain their ratio equal to a predetermined value; the mixture is then allowed to evolve during a phase of maturation so as to form a suspension; this suspension is separated into a liquid part from which are extracted the proteins having remained soluble, and a solid part containing proteins of different nature; and the parameters intervening in the proce

Abstract: A class of proteins associated with self-incompatibility alleles of plants, preferably of gametophytic self-incompatibility type, are provided. These proteins inhibit pollen tube growth in a plant style having the associated self-incompatibility allele, and have defined amino acid homologies and cross-reactivities.

Abstract: Microbially produced aprotinin and aprotinin homologs used for treating patients suffering from an excess release of pancreatic elastase, serum elastase or leukocyte elastase.

Abstract: A purified antigenic protein has been obtained which is capable of inducing in a chicken an immune response conferring protection against infection by Eimeria necatrix or Eimeria tenella. The protein has a molecular weight of about 26,000 and is composed of two polypeptides joined by a disulfide bond. The two polypeptide subunits have molecular weights of about 18,000 and about 8,000, respectively. The gene encoding the protein has been sequenced and the amino acid sequence of the protein deduced therefrom.The protein and antigenic polypeptides having an amino acid sequence included within the protein may be incorporated into a vaccine for conferring upon a chicken active immunity against infection by E. necatrix or E. tenella.

Abstract: A method of separating charged molecules having different numbers of charges thereon includes the step of passing the molecules to be separated through ion-exchange material such as an ion-exchange chromatograpy column in normal manner so that molecules to be separated bind to the ion-exchange material. Displacer molecules are then passed through the ion-exchange column to selectively release certain of the molecules to be separated from the ion-exchange material, while others of the molecules to be separated remain bound to the material.

Abstract: The particle size of amorphous protein material is reduced to uniform particulates without protein decomposition or loss of activity by passing the material through a fluid-energy mill.

Abstract: A method for the preparation of a protein in a physiologically active or native form, which method includesproviding a source of protein in a solubilized form,and a cationic exchange medium;contacting the source of protein and cationic exchange medium; andrecovering the protein in a physiologically active form.

Abstract: A method of preparing von Willebrand Factor by disassociating it from a chaotropic agent in solution therewith and preferably treating the same under controlled temperature either in liquid or lyophilized form.

Abstract: Stable pharmaceutical compositions suitable for parenteral administration to mammals are prepared which are in a pH range of about 2 to about 4 and comprise a therapeutically effective amount of a recombinant interferon-.beta. protein (IFN-.beta.) dissolved in an inert carrier medium comprising as a stabilizer/solubilizer an effective amount either of glycerol or of polyethylene glycol polymers having an average molecular weight from about 190 to about 1600 daltons. Further disclosed and claimed are methods for extracting IFN-.beta. from a microbial host transformed to produce it and then purifying and formulating said IFN-.beta. and methods for screening for other polyhydric non-detergent stabilizer/solubilizers or combinations thereof as solubilizer/stabilizers for pharmaceutical compositions of IFN-.beta..

Abstract: The present invention encompasses a method for removing proteins from a solution containing polynucleotides and proteins comprising filtering the solution through a nitrocellulose membrane at neutral or basic pH.

Abstract: A method for purifying a biologically active ligate. In this method, a ligand bonded to a first phase and having a specific affinity for the ligate is provided. The ligate is provided with a second phase. The first and second phases are then contacted together under conditions in which the ligand and ligate form a complex bonded to the first phase, with the ligand and ligate held together only by one or more non-covalent pressure sensitive bonds. At least a part of the second phase is then separated from the first phase to provide a purified first phase, and the purified first phase subjected to a pressure of at least 300 atmospheres under conditions sufficient to cause release of the ligate from the complex, but not sufficient to cause significant release of the ligand from the first phase. These conditions do not irreversibly cause biological activity of the ligate to be significantly reduced.

Abstract: The present invention discloses plant cells which contain modified 7S legume seed storage protein. Modification of 7S seed storage proteins which are expressible in plant cells and transformation of such genes into plant cells is also taught. Furthermore, methods and DNA molecules useful for producing plant cells containing modified 7S seed storage proteins are also disclosed. The invention is exemplified by insertion of an oligonucleotide encoding 15 amino acid residues, including 6 methionines, into a Phaseolus vulgaris phaseolin gene, thereby tripling its content of sulfur-containing amino acids.