Abstract: A group of growth factors, designated heparin-binding brain mitogens (HBBMs), is disclosed. The HBBMs are isolated from brain tissue by a sequence of purification steps.

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 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 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: Provided are PEGylated "interleukin-6" derivatives (PEG IL-6) having an extended plasma half-life, as well as enhanced in-vivo IL-6 biological activities.Methods for producing the modified glycosylated and unglycosylated IL-6 proteins or polypeptides, as well as, for their use in treating hematopoietic disorders and difficiencies, particularly acute thrombocytopenia, are also provided.

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 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: 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: A fused protein comprising a polypetide containing an antibody binding site of protein A and a polypeptide of lymphotoxin, and having biological activities of lymphotoxin and an ability to bind to an antibody is disclosed. Further, a process for the production of the fused protein, as well as a DNA coding for the fused protein, a plasmid containing the DNA, and E. coli transformed with the plasmid, necessary for the above-mentioned process, are provided.

Abstract: The present invention provides for a new polypeptide and a method for producing the same. The polypeptide has a molecular weight of approximately 30,000 daltons as a dimer and a monomer molecular weight of about 15,000 daltons, an isoelectric pH of about 4.47 and an activity of at least 21,000 units per milligram of protein in the monomer or dimer state. The preferred method comprises chromatographing a crude polypeptide-containing medium on a dextran derived chromatography column; precipitating the eluate in a water-ethanol solution; electrophoresing the precipitate in a polyacrylamide gel; and chromatographing the extract on a reverse phase-high performance liquid chromatography column.

Abstract: There is disclosed a human macrophage inflammatory protein-3 (MIP-3) and a human macrophage inflammatory protein-4 (MIP-4) polypeptides and DNA (RNA) encoding such polypeptides. There is also provided a procedure for producing such polypeptides by recombinant techniques and for producing antibodies against such polypeptides. In the invention there is also provided antagonist/inhibitors against such polypeptides which inhibit the functioning of such polypeptides. Another aspect of the invention provides a combination of the polypeptides of the present invention and a suitable pharmaceutical carrier for providing a therapeutically effective amount of the polypeptides for the treatment of various associated diseases.

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: 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.