Abstract: The present invention provides a process for the expression in appropriate host cells of recombinant DNA which is under the control of an inducible promotor. In order to obtain the soluble form of recombinant protein, which would usually be obtained in insoluble form, the induction of the promotor is limited to less than 10% of the maximum induction in comparison with a standard system and the transcription rate of the DNA coding for the protein is correspondingly limited.

Abstract: The invention relates to a non-glycosylated protein with enzymatic and serin protease activity, the zymogenous form thereof comprising the following domains of a protease of the factor IX family: (a) a catalytic domain, N-terminal bonded with (b) a zymogenous activation domain, N terminal bonded with (c) a EGF1 and/or EGF2 domain. Said protein can be used in a same way as the natural serine proteases of the factor IX family.

Abstract: A chimeric serine protease whose protease domain is composeD. of two domain halves (half-sides) with a &bgr;-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

Abstract: A chimeric serine protease whose protease domain is composed of two domain halves (half-sides) with a .beta.-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

Abstract: A peptide according to the present invention is not more than 40 amino acids long and contains a sequence which is at least 6 amino acids long from the amino acid partial sequence between the amino acids 144 and 183 of human .alpha.1-microglobulin or/and a sequence which is at least 6 amino acids long from the amino acid partial sequence between the amino acids 1 and 20 of human .alpha.1-microglobulin.An antibody according to the present invention is capable of specific binding to a peptide according to the present invention as well as to human .alpha.1-microglobulin.In order to determine human .alpha.1-microglobulin in a sample liquid by an immunoassay, the sample liquid is brought into contact simultaneously or sequentially with defined amounts of the components antibody and peptide whereby one of the components is labelled and the determination is carried out by means of this label.

Abstract: The invention relates to a process for recombinant preparation of peptides by expression of a DNA in micro-organisms, which DNA codes for a fusion protein made of streptavidin and one of the said peptides. Streptavidin and the peptide are bound by a peptide sequence which can be cleaved by an endoproteinase. The process also includes isolation of the insoluble, inactive protein, solublisation of the inactive protein using a denaturant, dilution of the denaturant at a pH value of between 8.5 and 11 until cleaving of the fusion protein by an endoproteinase can take place, cleaving of the fusion protein, lowering of the pH value until streptavin and non-cleaved fusion protein precipitate, and cleaning of the desired peptide from the supernatant. Said process is particularly suitably for producing parathromone and urodilatin and fragments thereof.

Abstract: An electrochemical sensor is provided containing a supporting material having a surface of noble metal such as gold or palladium to which is bound an enzyme such as glucose oxidase via binding molecules. The binding molecules are in the form of a homogenous monolayer and are bound to the metal surface by anchor groups such as thiol, disulphide or phosphine groups. The enzyme is linked to the binding molecules by an ionic bond, a covalent bond or a metal-chelate bond. The binding molecules may contain a spacer such as an alkylene chain. Coverage of the binding molecules on the metal surface is less than the maximum coverage to optimize enzyme coverage, decrease response time of the sensor and increase signal yield per surface area. The monolayer may contain diluent molecules which are not linked to an enzyme and which are bound to the metal surface via anchor groups.

Abstract: Saccharomyces mutants with defects in N-glycosylation which are obtainable by ?.sup.3 H!-mannose suicide selection, introduction of one or several selective markers, selection of those strains which, after transformation with the plasmid YEpL/glucose oxidase, secrete 10 mg/l glucose oxidase or more into the culture medium after culture under standard conditions, are allelic to the ngd mutations in Saccharomyces cerevisiae, DSM 7042, DSM 7338, DSM 7160 and/or 7340 and express proteins with a uniform carbohydrate structure.

Abstract: Saccharomyces mutants with defects in N-glycosylation which are obtainable by ?.sup.3 H!-mannose suicide selection, introduction of one or several selective markers, selection of those strains which, after transformation with the plasmid YEpL/glucose oxidase, secrete 10 mg/l GOD or more into the culture medium after culture under standard conditions, are allelic to the ngd mutations in Saccharomyces cerevisiae, DSM 7042, DSM 7338, DSM 7160 and/or 7340 and express proteins with a uniform carbohydrate structure.

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: Hypoglycosylated recombinant glucose oxidase with a molecular weight of ca. 68-80 kDa, a specific activity of ca. 200 U/mg unit of weight, a carbohydrate portion of ca. 12% which is obtainable by expression of a recombinant DNA containing the GOD gene in the N-glycosylation-defective yeast mutants DSM 7042, DSM 7338, DSM 7160 or DSM 7340 or allelic mutant strains, fermentation and isolation of the enzyme from the culture supernatant or the cells.

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: 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: A fusion protein with at least one antigenic and/or immunogenic determinant from the env, gag and/or pol region of HIV1 and/or HIV2 which contains the tetrapeptide sequence NH.sub.2 -Met-Tyr-Tyr-Leu as the N-terminal component as well as a process for its production and use.

Abstract: The present invention provides a process for the production of proteins or protein-containing gene products by transformation of eukaryotic host cells with a recombinant DNA molecule containing the gene for the desired protein, culturing the cells and isolating the gene product after expression, wherein, as host cells, there is used a yeast strain which is deficient in proteases A and B.