Abstract: A process is disclosed for continuously treating a solubilized protein solution containing a protein unfolded to some degree, in a small volume continuous flow reactor, to obtain the protein in a conformation exhibiting the protein's characteristic biological activity by continuously diluting out the solubilizing agent, while continuously withdrawing the refolded protein. The continuous process may be carried out using deionized water as a diluent, rather than buffer solutions.

Abstract: Treating composition and method for biological control of corn seed rots and seedling blights. The composition comprises a culture of emulsifier and surfactant producing bacteria selected from the strains of 6519EO1, 6133DO2, 6109DO1, and their respective genetic equivalents and a carrier. The composition is applied to seeds or the aqueous media surrounding seeds in plant growth media to prevent corn seed rot and seedling blight.

Abstract: A method for the recovery of proteins in a solubilized form from host cells including providing a source of host cells incorporating a synthesized or expressed protein; providing a source of at least one cationic surfactant; and treating the host cells with at least one cationic surfactant, in an amount sufficient to effect solubilization of the proteins.

Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight contaminating proteins by directly adding Group IIA metal salts 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: Reactivation of cysteine-containing protein in a process, in which a reduced and denatured cysteine-containing protein such as salmon growth hormone I or eel growth hormone I can be efficiently reactivated.

Abstract: Protein A is selectively isolated from an antibody--Protein A mixture by exposing the mixture to an anion exchange material under conditions sufficient to adsorb both components and then sequentially eluting the antibodies and protein A under conditions of increasing ionic strength. Resulting antibody preparations have less than about 15 ng of Protein A per mg of antibody.

Abstract: A method of purifying a recombinant protein from a solution, such as tissue culture fluid, containing gylcoproteins. The affinity of lectins for specific glycoproteins is assessed and used to select a particular lectin specific for the contaminating glycoprotein(s). A sugar buffer such as alpha methyl mannoside prevents binding of the recombinant protein. The preferred lectin is lentil lectin, for use in separating recombinant Factor VIII from tissue culture fluid contaminated with rodent protein from the cell line used to produce the recombinant Factor VIII.

Abstract: The recovery of vitamin K-dependent proteins produced by transformed microorganisms can be effected from the cell culture medium utilizing the changes in the protein which occur in the presence of divalent cations. The present process uses divalent cations to alter the binding affinity of the proteins and thereby selectively elute the proteins away from contaminants in the culture medium using standard chromatography.

Abstract: Disclosed is a method of recovery of antihemophilic factor (AHF) from human plasma by precipitation with citric acid, sodium citrate, or potassium citrate.

Abstract: A method of recovering biologically active somatotropins which are produced as insoluble refractile bodies in transformed microorganisms which comprises dissolving refractile bodies in a denaturant and 2-amino-2-methyl-1-propanol, homogenizing, and diluting to fold.

Abstract: Nuclear polyhedrosis viruses, for example, Autographa californica nuclear polyhedrosis virus (AcMNPV), useful in the control of lepidopterous larvae such as the larvae of the cabbage looper Trichoplusia ni, have been found to have enhanced infectivity when mixed with certain proteins obtained from the granulin fraction of Trichoplusia ni granulosis virus (TnGV) or Heliothis armigera granulosis virus (HaGV), and from the polyhedrin fraction of AcMNPV viruses. The proteins from the TnGV granulin fraction have molecular weights of about 101 and about 104 kd. The enhanced infectivity is correlated to biochemical and structural changes in the T.ni peritrophic membrane.

Abstract: A method for the preparation of proteins in biologically active form including providing a source of protein solubilized from inclusion bodies with a cationic surfactant; providing a weak denaturing agent; and contacting the solubilized protein with the weak denaturant in water in an amount sufficient to allow the protein to remain in a biologically active form.

Abstract: A process for the preparation of a spatial form, which has biological activity, of a protein from a biologically inactive spatial form is described and comprises the protein being dissolved with the addition of a denaturing agent and thus converted into the random coil form, and the solution being allowed to pass through a material which has molecular sieve properties and contains a liquid medium in which the protein can assume a spatial form which has biological activity, and this material having molecular sieve properties being selected so that the molecules of the denaturing agent can penetrate, but the protein molecules canot. It is possible by centrifugation, blowing or sucking out to remove the medium in the "external volume" of the molecular sieve and to increase the rate of passage of the solution through the molecular sieve.

Abstract: The present invention discloses a new method for solubilizing and refolding recombinant proteins expressed as granules. The method involves sulfitolysis and the formation of a precipitate of protein-S-sulfonate by warming. The precipitate has been found to contain protein in high purity. In addition, proper folding takes place if the desired protein is fully reduced and passed through an intermediate concentration of denaturant which allows for a transition between its folded and unfolded states.

Abstract: There is disclosed a method for purifying a gene-expression product produced by recombinant DNA technique which comprises a specific sequence of steps including adsorption treatment with silica gel, adsorption treatment with activated carbon, at least twice density gradient centrifugation and at least twice equilibrium density gradient centrifugation. The method of the present invention is very effective to remove allergen from gene-expression products contaminated therewith, enabling highly purified gene-expression products to be produced on a large scale.

Abstract: Disclosed are ultrafiltration processes for the enrichment and concentration of selected proteins from protein conaining fluids. Illustratively, IgG is concentrated from whey by means of multiple ultrafiltration "passes", using a metallic oxide ultrafiltration membrane, which are characterized by differing pH's.

Abstract: Immunologically intact protein or peptide immunogens are recovered from vaccines consisting of immunogen-aluminum hydroxide (alum) complexes. Recovery consists of dissolution of the complexes with an alkali metal salt of a carboxylic acid at a basic pH, reduction of the pH to physiological levels, removal of excess dissolvent and isolation of the protein or peptide immunogen.