Abstract: A respiratory delivery system is disclosed which preferably includes both medicament and plower recharge capabilities. The system includes a portable inhaler with a rechargeable medicament cartridge and a rechargeable power supply. This power supply may be electrically interconnected with one or more components of the portable inhaler, including a droplet ejection device, a controller for the droplet ejection device, an actuation switch, an inhalation sensor, and/or an electronic memory. The system further includes a recharging unit which includes an inhaler docking station, a medicament recharging system, and a power recharging system. When the portable inhaler is docked to the recharging unit, the recharging unit recharges the power supply of the portable inhaler and recharges the medicament cartridge of the portable inhaler by providing additional medicament thereto.

Abstract: An improved process for recovering and purifying lipophilic recombinant proteins such as human .beta.-interferon from their hosts involves concentrating the bacteria; disrupting the cell wall and solubilizing the protein into an aqueous medium with an appropriate solubilizing agent; extracting the protein from the aqueous medium with 2-butanol, 2-methyl-2-butanol or mixtures thereof; precipitating and isolating the protein from the alcohol phase; purifying the protein by chromatography and diafiltering the protein against distilled water or aqueous solutions of ethanol or glycerol at a pH of about 12. Therapeutic formulations of such purified proteins with stabilizers contain SDS levels reduced to less than 10 p.p.m.

Abstract: Highly stable, pharmaceutical compositions comprising a therapeutically effective amount of a biologically active recombinant lipophilic protein such as human .beta.-interferon and interleukin-2 dissolved in a non-toxic, inert, therapeutically compatible aqueous-based carrier at pH ranges of from about 6.8 to 7.8 and about 8.5 to 10, which formulations contain a stabilizer for the protein selected from the group comprising human serum album, human serum albumin and dextrose or human plasma protein fraction, and at a pH range of from about 2 to 4, which latter formulations optionally contain a carbohydrate and/or protein stabilizer, are disclosed. Further, preferred formulation processes to prepare said compositions are described which avoid highly alkaline conditions.

Abstract: An improved process for recovering and purifying lipophilic recombinant proteins such as human .beta.-interferon and interleukin-2 from their hosts yields a protein preparation which may be formulated into a stable pharmaceutical composition having a therapeutically effective amount of the biologically active recombinant lipophilic protein dissolved in a non-toxic, inert, therapeutically compatible aqueous-based carrier medium at a pH of 6.8 to 7.8 which medium also contains a stabilizer for the protein, such as human serum albumin, normal serum albumin and human plasma protein fraction.

Abstract: A process is disclosed for the purification of recombinantly produced biologically active proteins in which a solution containing a mixture of materials, including the biologically active protein, is passed through a continuous porous hydrophobic membrane, and the fraction enriched in the biologically active protein is recovered. Hydrophobic proteins such as TNF and recombinant ricin toxin A chain may be purified according to the process. Conditions for enhanced recovery of purified TNF using the process are disclosed. A highly purified TNF comprising 95% or greater TNF as determined by SDS-PAGE analysis, with an endotoxin content of less than 0.1 ng/mg TNF which is substantially free of pyrogens by the USP rabbit pyrogen test at a dosage range of 1.0 to 2.4.times.10.sup.5 U/kg, is obtained.

Abstract: A refractile material containing a heterologous protein is recovered from a host microorganism cell culture transformed to produce the protein. One recovery process involves disrupting the cell wall and membrane of the host cell, removing greater than 99% by weight of the salts from the disruptate, redisrupting the desalted disruptate, adding a material to the disruptate to create a density or viscosity gradient in the liquid within the disruptate, and separating the refractile material from the cellular debris by high-speed centrifugation. Another version of such a recovery process comprises the further steps of solubilizing the refractile material under reducing conditions, organically extracting the solubilized refractile material, and isolating said refractile material from the extractant.Preferably the protein is recombinant IL-2 or IFN-.beta. and the salt removal step is carried out by diafiltration.

Abstract: An improved process for recovering and purifying .beta.-HIFN from transformed bacterial comprising concentrating the bacteria; disrupting the cell wall and solubilizing the .beta.-HIFN into an aqueous medium with an appropriate solubilizing agent; extracting the .beta.-HIFN from the aqueous medium with 2-butanol, 2-methyl-2-butanol or mixtures thereof; precipitating and isolating the .beta.-HIFN from the alcohol phase; purifying the .beta.-HIFN by chromatography and diafiltering the .beta.-HIFN against distilled water or aqueous solutions of ethanol or glycerol at a pH of about 12; and therapeutic formulations and compositions of .beta.-HIFN within SDS levels therein reduced to less than 10 p.p.m.