Abstract: A prefabricated tympanic membrane prosthesis includes a piece of collagen sheet processed with a diluted solution of formalin. The piece of collagen sheet is molded on a forming surface of a tool having a shape resembling a natural tympanic membrane of a human subject. The piece of collagen sheet is processed with a diluted solution of formalin so that the resulting tympanic membrane prosthesis retains the shape of the forming surface. The tympanic membrane prosthesis is semi-rigid, yet flexible, and is packaged in a substantially rigid container to protect it shape during shipment and storage.

Abstract: A method of recovering a purified and stabilized protein having antihemophilic factor activity (Factor VIII), from a biological sample containing Factor VIII, at least one destabilizing protease impurity, i.e. thrombin, and optionally one or more proprotease impurity, is provided. The biological sample is contacted with a protease removing and/or inhibiting agent, thereby inhibiting and/or removing the destabilizing protease impurity. The method provides increased yield and resolution of Factor VIII. Also provided are purified and stabilized Factor VIII non-lyophilized, liquid in compositions.

Abstract: A method of recovering a purified and stabilized protein having antihemophilic factor activity (Factor VIII), from a biological sample containing Factor VIII, at least one destabilizing protease impurity, i.e. thrombin, and optionally one or more proprotease impurity, is provided. The biological sample is contacted with a protease removing and/or inhibiting agent, thereby inhibiting and/or removing the destabilizing protease impurity. The method provides increased yield and resolution of Factor VIII. Also provided are purified and stabilized Factor VIII non-lyophilized, liquid in compositions.

Abstract: Disclosed are conjugates of a protein having antihemophilic factor (Factor VIII) activity linked to nonantigenic ligands. The conjugates have longer half life than the unconjugated protein but maintain substantial Factor VIII activity.

Abstract: Disclosed are methods for purifying proteins including AHF by column chromatography in the presence of additives including sugars and polyhydric alcohols which serve to increase the electrostatic forces on the surface of said proteins while decreasing the hydrophobicity of said proteins resulting in preparations of such proteins of high purity and/or resolution and/or recovery.

Abstract: The present invention relates to a high-recovery, high-resolution method for purifying antihemophilic factor by using column chromatography techniques in the presence of sugars, polyhydric alcohols, amino acids or salts.

Abstract: Disclosed are methods for purifying proteins including AHF by column chromatography in the presence of additives including sugars and polyhydric alcohols which serve to increase the electrostatic forces on the surface of said proteins while decreasing the hydrophobicity of said proteins resulting in preparations of such proteins of high purity and/or resolution and/or recovery.

Abstract: Proteins and non-protein affinity ligands are covalently bonded to trichloro-s-triazine activated supports. The activated support is prepared by reacting a water-free insoluble solid support with trichloro-s-triazine in a non-aqueous medium and neutralizing HCl generated during the reaction with a tertiary amine which does not form an insoluble complex with the trichloro-s-triazine.

Abstract: An affinity chromatography method for the separation and pruification of two active forms of urokinase from a crude urokinase preparation. The method employs an extracting agent of agmatine covalently coupled to the surface of a water-insoluble solid support material such as agarose, and three separate specific buffer solutions. A low ionic strength buffer, such as 0.01 molar sodium phosphate buffer, pH 6.0-9.0, is used in preparing the loading solution and for washing the extracting agent. A slightly higher ionic strength buffer, such as 0.02 molar sodium phosphate buffer, pH 6.0-9.0, is used as a first eluant for eluting from the extracting agent a first active form of urokinase which is characterized by a molecular weight of approximately 33,400 and a specific activity of approximately 226,000 CTA units/mg protein. A still higher ionic strength buffer with added salt, such as 0.1 molar sodium phosphate -- 0.4 molar sodium chloride buffer, pH 5.0-8.