Abstract: The present invention concerns a process for the isolation of recombinant IgA protease from inclusion bodies. In addition a recombinant DNA is claimed which codes for an IgA protease whose C-terminal helper sequence and preferably also its N-terminal signal sequence is no longer active.

Abstract: Aqueous pharmaceutical preparations of G-CSF are disclosed that are stable on storage and a buffer selected from the group consisting of a salt of citrate, maleate, a combination of phosphate and citrate, and arginine; and at least one surfactant.

Abstract: The present invention concerns lyophilized pharmaceutical preparations of G-CSF that contain maltose, raffinose, sucrose, trehalose or amino sugar as stabilizing agents. In additon the invention concerns a process for the production of stabilized lyophilisates as well as the use of maltose, raffinose, sucrose, trehalose or amino sugar as stabilizing agents of pharmaceutical agents containing G-CSF.

Abstract: The present invention concerns a process for the isolation of recombinant core streptavidin in which host cells are transformed with a DNA coding for core streptavidin, the transformed host cells are cultured under suitable conditions, the DNA coding for core streptavidin is expressed and the recombinant core streptavidin is isolated from the host cells or the culture medium, wherein a DNA coding for core streptavidin is used which has(a) the nucleotide sequence shown in SEQ ID NO. 1 or(b) a nucleotide sequence corresponding to the nucleotide sequence (a) within the scope of the degeneracy of the genetic code.

Abstract: The invention concerns a process for the reactivation of denatured protein, in which the protein is incubated with a solution of Tris base or/and a salt of Tris at a concentration of at least 400 mmol/l and at a pH at which the protein to be treated can take up its native conformation.

Abstract: A process for the activation of disulphide linked recombinant proteins expressed in prokaryotes is described. The process includes cell digestion, solubilization under denaturing and reducing conditions and activation under oxidizing conditions in the presence of GSH/GSSG and a non-denaturing amount of a denaturing agent.

Abstract: A process for the activation of recombinant proteins which are present in at least a partially inactive form in which a protein is activated by known solubilization or/and renaturation techniques, said protein having additional helper sequences 2 to 50 amino acids in length at its N- or/and C-terminus whereby the relative hydrophobicity of these helper sequences which is calculated as the sum of the relative hydrophobicity specified in Table 1 for the individual amino acids has a negative numerical value.

Abstract: The present invention concerns a process for the isolation of recombinant core streptavidin in which host cells are transformed with a DNA coding for core streptavidin, the transformed host cells are cultured under suitable conditions, the DNA coding for core streptavidin is expressed and the recombinant core streptavidin is isolated from the host cells or the culture medium, wherein a DNA coding for core streptavidin is used which has(a) the nucleotide sequence shown in SEQ ID NO. 1 or(b) a nucleotide sequence corresponding to the nucleotide sequence (a) within the scope of the degeneracy of the genetic code.

Abstract: The present invention concerns a method for the stabilization of proteins in an aqueous solution which is characterized in that one or several members of the heat shock protein (Hsp90) family are added to the aqueous solution containing protein.

Abstract: A process for the activation of t-PA or IgG after expression in prokaryotes is described. The process includes cell digestion, solubilization under denaturing and reducing conditions and activation under oxidizing conditions in the presence of GSH/GSSG.

Abstract: In a process for the production of recombinant, biologically active, eukaryotic alkaline phosphatase a DNA sequence coding for a eukaryotic alkaline phosphatase is expressed in a prokaryotic host cell and the expression product is obtained in an active form by cell lysis, solubilization under denaturing conditions and subsequent renaturation. In this process the renaturation step is carried out in the presence of one or several stabilizing agents.

Abstract: The invention is a pharmaceutical composition containing a glycosylated protein having human tissue type plasminogen activator activity of at least 1.4 MU/ml, citrate, and at least one of a number of various compounds. The composition has a pH ranging from 4.5 to 9.

Abstract: Pharmaceutical preparation of a protein with t-PA activity with an enzymatic activity of at least 0.25 MU/ml. and a pH value of 4.5 to 9 which contains a substance of the group citric acid, ascorbic acid, 2-oxoglutaric acid, fumaric acid, Tris and EDTA in a concentration of at least 0.2 mole/l., as well as a medicament based on a protein with t-PA activity and processes for its preparation.

Abstract: Pharmaceutical compositions containing non-glycosylated human tissue type plasminogen activator (t-PA) having enzymatic activity of at least 0.1 MU/ml are disclosed. The compositions have a pH of from 4.5 to 6, contain citrate, and at least one other compound.

Abstract: Stabilized compositions containing a non-glycosylated human tissue type plasminogen activator derivative are disclosed. The derivative is referred to as K2P pro. The composition has enzymatic activity of at least 1.1 mU/ml, a pH of from 4.5 to 6.5, and contains citrate as well as at least one of a variety of different compounds.

Abstract: A new thrombolytically active protein is not glycosylated and consists of the following amino acid sequence: ##STR1## or said amino acid sequence with an additional N-terminal methionine. DNA sequences encoding the thrombolytically active, non-glycosylated protein and pharmaceutical compositions containing said protein are also disclosed. The protein possesses particularly favorable properties when used to dissolve blood clots.

Abstract: The present invention provides a process for the activation of gene-technologically produced, biologically active proteins expressed in prokaryotes after cell digestion by solubilization under denaturing conditions and reducing conditions and subsequent reactivation under oxidizing and renaturing conditions, wherein working is carried out at a protein concentration of 1 to 1000 .mu.g./ml. and, between the solubilization and the reactivation, a dialysis is carried out against a buffer with a pH value of from 1 to 4 containing 4 to 8 mole/liter guanidine hydrochloride or 6 to 10 mole/liter urea.

Abstract: The present invention provides a process for the renaturation of denatured proteins in solution in a renaturation buffer, wherein a solution is prepared of the protein to be renatured in the critical concentration in a selected buffer and, after formation of the folding intermediate, further protein to be renatured is added in the amount necessary for the achievement of the critical concentration.

Abstract: To permit connecting a display characterizing a malfunction, for example malfunction in an automotive vehicle, or another monitored apparatus, and a warning lamp to alert an operator that a malfunction is being indicated to a single connecting line (SL), a coded representation characterizing the malfunction in the form of short pulses (I; 1, 2) is transmitted on the same line, with pulses which are so short that the response inertia of the warning lamp does not perceptively change its brightness (or darkness) level, as controlled by the operating voltage of the warning lamp between a high and a low value. The coded pulse representation is decoded in a microprocessor (MP) and displayed on a display (A) forming part of an evaluation device, coupled to the same single communication line (SL) which may be a single wire with chassis or ground return, or a two-wire connection.