Abstract: Methods for purifying factor VIII:C, von Willebrand factor (vWF) or complexes thereof from heterogeneous biological fluids are disclosed. The methods utilize a binding peptide, specific to either factor VIII:C or vWF, bound to an insoluble matrix. Peptides suitable for use within the methods are also disclosed.

Abstract: A process for the preparation of albumin which has extremely low levels of or is essentially free of colorants, metal ions, human proteins, fragments of albumin, polymers or aggregates of albumin, and viruses, and which is relatively non-glycated, relatively high in free thiol and with an intact C-terminus. The process comprises passing albumin (preferably expressed and secreted by transformed yeast) through two chromatography purifications, ultrafiltering the product, passing through two further chromatography steps and again ultrafiltering the product.

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 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: 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 non-toxic and non-cytolytic derivative of streptolysin O which retains at least one (preferably immunodominant) epitope is produced, and can be used especially in diagnostic tests for detecting of the presence of antibodies to Streptococcus pyogenes in a sample.

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 relates to a method for isolating and purifying transferrin and lactoferrin receptor proteins from bacterial pathogens by affinity chromatography and to vaccine antigens containing the purified receptor proteins.

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: A purified protein, factor J, which has inhibitory properties which prevent the formation or the dissociation of Cl complex and a method of purification for said protein. The method including the following sequential chromatography steps: anion exchange, QAE-"SEPHADEX", heparin-"SEPHAROSE" affinity, "MONO Q" and hydroxylapatite.

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: Purification of human FSH from post-menopausal urine gonadotropin using immunoaffinity chromatography with elution at high pH and reverse-phase HPLC steps yields a biologically active hormone which is free from detectable traces of luteinizing hormone and other urinary proteins.

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 purified protein, factor J, which has inhibitory properties which prevent the formation or the dissociation of Cl complex and a method of purification for said protein. The method including the following sequential chromatography steps: anion exchange QAE-"SEPHADEX", heparin-"SEPHAROSE" affinity, "MONO Q" and hydroxylapatite.

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: 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 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: 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 isolating cell surface receptors utilizing a short peptide sequence bound to an affinity column. Cell surface receptors which bind selectively to the short peptide and which are specific to various adhesion proteins may be isolated therewith from various cell preparations. These receptors, whose functional integrity has been maintained by the presence of the peptide ligand, are incorporated into liposomes and used to deliver specific compounds inside the liposomes to select tissues containing the specific adhesion proteins.

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.