Abstract: A new glycoprotein ZP-0 originating from the oviduct of a mammal having a molecular weight of about 200,000 to 240,000, as determined by SDS-polyacrylamide gel density-gradient electrophoresis having an isoelectric point of about 4 to 6.2, as determined by isoelectric focusing, containing no sub-fragments, as determined by SDS-disk electrophoresis, forming a carbamylation train in two-dimensional electrophoresis (isoelectric focusing, and SDS-polyacrylamide gel density-gradient electrophoresis), and facilitating species-specific bonding of sperm to zonae pellucidae; and a process for production of the above-mentioned glycoprotein comprising, preparing oviduct from a mammal, homogenating the oviduct optionally with a buffer, to obtain a homogenate, obtaining a liquid containing the glycoprotein from the homogenate, adsorbing the glycoprotein onto lectin immobilized on an insoluble support, liberating the gylcoprotein from the support, and recovering the glycoprotein.

Abstract: The chemically modified protein of the present invention has a strong islet-activating activity and is lower in various side effects than non-modified IAP, so that it may be employed as a prevention and therapeutic drug for diabetes.

Abstract: A course of a parasitic, e.g. protozoal, infection is combated by administering to the host an immunomodulating effective amount of a calf thymus hormone extract.

Abstract: This application describes a process for selectively cleaving a peptide or protein at one or more of its tryptophan residues. The process comprises treating in trifluoroacetic acid said peptide or protein at a concentration of from about 0.05 mM to about 50 mM with an organic sulfoxide at a concentration of from about 0.01M to about 1M, chloride ion at a concentration of from about 0.01M to about 2M, and water at a concentration not in excess of about 10M.

Abstract: A method for solubilization and naturation of somatotropin protein from refractile bodies of host cells is disclosed. The method embraces the discovery that an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, can be effectively used to solubilize refractile bodies containing such somatotropin protein. Once solubilized, somatotropin protein can be natured in an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, by contacting the solution with a mild oxidizing agent for a time sufficient to result in the formation of the disulfide bonds. Naturation can efficiently occur even at high protein concentration, in an impure preparation and in the absence of reducing agent.

Abstract: A conjugate of 9-(2-hydroxyethoxymethyl)-guanine with lactosaminated human albumin is therapeutically more efficacious than the free drug in the treatment of chronical hepatitis induced from Virus B. For the preparation of the conjugate an aqueous solution of 9-(2-hydroxyethoxymethyl)-guanine in form of a derivative, particularly monophosphate, and an aqueous solution of lactosaminated human albumin are reacted in the presence of 1-ethyl-3-(dimethylaminopropyl)-carbodiimide, by adjusting the pH to the value of 7.5 and by maintaining the reaction mixture for 24 hours under stirring and in the dark.

Abstract: Compositions containing therapeutically or immunologically active proteins are rendered substantially free from infectious agents such as viable viruses and bacteria without substantial loss of therapeutic or immunologic activity by mixing the protein composition with a complex formed from transition metal ions, such as copper ions, and an angularly-fused, polynuclear heterocyclic arene having two nitrogen atoms in a "cis-ortho" relationship, such as phenanthroline, and a reducing agent such as a thiol or ascorbic acid or ascorbate salt or mixtures of ascorbic acid or ascorbate with a thiol in amounts and at a temperature and for a time sufficient to inactivate substantially all of the viruses and bacteria contained therein. Compositions containing therapeutically active proteins substantially free from viral and bacterial infectivity, which have heretofore been unattainable, can be prepared by the method of the invention.

Abstract: Glycoproteinic conjugates having trivalent immunogenic activity obtained by binding, by a covalent bond, to a protein selected among CRM 197, tetanus toxoid, and pertussis toxin, at least an oligosaccharidic hapten derived from the capsular polysaccharide of a gram-positive bacterium and at least an oligosaccharidic hapten derived from the capsular polysaccharide of a gram-negative bacterium, and wherein said oligosaccharidic haptens are previously activated by introducing terminal esters.

Abstract: Monomeric, biologically active growth hormone is isolated from microbially-produced insoluble inclusion bodies by solubilizing and denaturing the growth hormone by extraction of the inclusion bodies into a guanidine salt solution such as guanidine hydrochloride and subsequently renaturing at least a portion of the growth hormone in the solution by replacing the guanidine salt solution with a denaturant-free buffer solution and removing precipitated impurities and growth hormone aggregates. The renatured growth hromone is then purified by ion-exchange chromatography.

Abstract: A method for solubilization and naturation of somatotropin protein from refractile bodies of host cells is disclosed. The method embraces the discovery that an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, can be effectively used to solubilize refractile bodies containing such somatotropin protein. Once solubilized, somatotropin protein can be natured in an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, by contacting the solution with a mild oxidizing agent for a time sufficient to result in the formation of the disulfide bonds. Naturation can efficiently occur even at high protein concentration, in an impure preparation and in the absence of reducing agent.

Abstract: A method for purifying erythropoietin is described. The method comprises treating partially purifying erythropoietin by reverse phase high performance liquid chromatography to obtain homogeneous erythropoietin having a molecular weight of about 34,000 daltons on SDS PAGE and moving a single peak on reverse phase HPLC. The homogeneous erythropoietin protein preferably has a specific activity of at least 120,000 IU, more preferably at least 160,000 IU per absorbance unit at 280 nm.

Abstract: Chromatographic procedures are individually and jointly applied to the rapid and efficient isolation of biologically active proteins and especially glycoproteins such as recombinant erythropoietin present in the medium of growth of genetically transformed mammalian host cells. Illustratively, recombinant EPO is isolated from culture fluids by reverse phase chromatography employing a C.sub.4 or C.sub.6 column and elution with ethanol. Recombinant erythropoietin may also be purified by anion exchange chromatography employing, e.g., a DEAE resin, with preliminary selective elution of contaminant materials having a lower pKa than erythropoietin from the resin under conditions mitigating against acid activated protease degradation. Practiced serially, the two chromatographic procedures allow for high yields of biologically active recombinant erythropoietin from mammalian cell culture media.

Abstract: Method of inhibiting the adhesion of Bordetella pertussis to the cilia of human respiratory cells to treat pertussis, agents and compositions useful in the method. Agents are also useful to stimulate the production of antibodies.