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 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: 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: 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: 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: Substantially pure proteins active in humoral hypercalcemia of malignancy (PTHrP) and sub-units and fragments thereof. Antibody reagents capable of binding to epitopes of PTHrP. Methods and kits for the detection of PTHrP.

Abstract: The present invention relates to the application, as the stationary phase in affinity chromatography for the purification of the FGF type growth factors, of the polymers or copolymers onto which --SO.sub.3 H and --SO.sub.3 M groups are randomly bound, groups in which M denotes a physiologically acceptable metal, as well as, preferably, --SO.sub.2 R groups, in which R denotes a radical obtained by removal of a hydrogen atom from the amino group of an amino acid or an amino acid derivative.The invention relates also to the obtaining of a purified bFGF or aFGF growth factor, or a mixture of these growth factors, consisting in carrying out an affinity chromatography on a resin such as defined hereinabove, by carrying out an elution with a neutral pH buffer having an ionic strength equivalent to that of a 0.15 M to 2.5 M NaCl solution.

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: 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. The growth factors may be useful in the promotion of angiogenesis, such as in the promotion of wound healing, bone healing and in the treatment of burns, as well as in promoting the formation, maintenance and repair of tissue, in particular, neural tissue.

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 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: 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: A method for recovering a recombinant protein from a protein solution containing high molecular weight containing proteins by directly adding amine or quaternary ammonium compounds to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants.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: 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: The invention relates to the purification and characterization of growth stimulatory and inhibitory protein factors produced by various organs which appear to play a role in the successful formation of metastatic colonies of tumor cells. In particular, it has been found that syngeneic organs secrete protein growth stimulatory and inhibitory factors which can, at low concentrations, affect metastatic tumor cells. The ability of a malignant cell to respond to these factors is believed to be related to tumor cell metastasis to specific body organs. In particular a lung growth stimulatory glycoprotein having a molecular weight of approximately 66,000 daltons has been found to stimulate growth of lung-metastatic rat and human mammary tumor cells in serum deprived medium.