Abstract: A mini-proinsulin, in which the amino acid Arg bridges the A and the B chain instead of the C chain, shows insulin activity and is suitable for the preparation of pharmaceuticals for the treatment of diabetes mellitus. It can furthermore be converted into an insulin derivative simply using trypsin, the B chain of which is lengthened by Arg. This can be converted into insulin using carboxypeptidase B. Advantageously, however, the mini-proinsulin can also be converted to insulin directly in a one-pot process.

Abstract: The present invention relates to novel hIL-4 mutant proteins, to processes for preparing them, and to their use as medicaments, in particular in overshooting, falsely regulated immune reactions and autoimmune diseases.

Abstract: New insulin derivatives of the formula II with an iso-electric point between 5 and 8.5, with improved stability in weakly acid aqueous medium and with a special action profile, and the physiologically tolerated salts of these insulin derivatives, for the treatment of diabetes mellitus; formula II is: ##STR1## in which R.sup.1 denotes H or H-Phe,R.sup.2 denotes a genetically encodable L-amino acid which contains no amide group,R.sup.30 represents the residue of a neutral genetically encodable L-amino acid,R.sup.31 represents a physiologically acceptable organic group which is basic in nature and has up to 50 carbon atoms, in whose structure 0 to 3 .alpha.-amino acids are involved and whose terminal carboxyl group which is present where appropriate can be free, in the form of an ester functionality, an amide functionality, a lactone or reduced to CH.sub.2 0H, andX represents a genetically encodable L-amino acid.

Abstract: A process is described to specifically hydrolyze the amino acid chain of preproinsulin analogs to give the corresponding insulins. The hydrolysis is catalyzed by clostripain and, if necessary, carboxypeptidase B.

Abstract: The invention relates to a process for preparing recombinant aprotinin and recombinant aprotinin variants having the natural N-terminal sequence, with the recombinant aprotinin and/or the recombinant aprotinin variants being present as homogeneously processed, secreted proteins.

Abstract: New insulin derivatives, the use thereof, and a pharmaceutical composition containing themInsulin derivatives having an isoelectric point between 5 and 8.5, or physiologically tolerated salts thereof, of the Formula II ##STR1## in which: R.sup.1 at position B1 denotes H or H-Phe;R.sup.2 at position A21 denotes a genetically encodable L-amino acid selected from the group consisting of Gly, Ala, Val, Leu, Ile, Pro, Phe, Trp, Met, Ser, Thr, Cys, Tyr, Asp, and Glu;R.sup.30 represents the residue of a neutral genetically encodable L-amino acid selected from the group consisting of Ala, Thr, and Ser;R.sup.31 represents 1, 2, or 3 neutral or basic alpha amino acids, wherein at least one of the alpha amino acids is selected from the group consisting of Arg, Lys, Hyl, Orn, Cit, and His;X represents His at position B10; andthe sequences A1 to A20 and B1 to B29 in Formula II correspond to a mammalian insulin;excluding those insulin derivatives in which simultaneously:R.sup.1 at position B1 denotes Phe; andR.sup.

Abstract: The invention relates to a method for the preparation of polypeptides or proteins by enzymatic cleavage of the oligo- or polyglycine sequence of a fusion protein using an endoprotease.

Abstract: Pharmaceutical formulations for the treatment of diabetes mellitus are disclosed, wherein the pharmaceutical formulations contain at least one insulin derivative modified with a base in position B31 of the insulin B chain and having an isoelectric point between 5.8 and 8.5 and/or at least one of its physiologically tolerated salts in a pharmaceutically acceptable excipient and a relatively high zinc ion content in the range from above 1 .mu.g to about 200 .mu.g of zinc/IU. The preferred insulin derivative modified with a base for this pharmaceutical formulation is human insulin-B31-Arg-OH and human insulin-B31-Arg-B32-Arg-OH. The formulation is used for the treatment of diabetes mellitus; it has a particularly favorable action profile.

Abstract: Basic proteins are isolated from protein mixtures which contain such basic proteins and which are obtained by enzymatic clevage of proinsulin and/or its derivatives of natural, semisynthetic or genetic engineering origin by ion exchanger chromatography on strongly acid cation exchangers.

Abstract: Mixed crystals composed of (a) unmodified insulin, des-Phe-B1 insulin, des-Thr-B30 (human) or des-Ala-B30 (pork, beef) insulin and (b) least one insulin having a basic modification at the C-terminal end of the B chain, preferably composed of human insulin and Arg-B31 human insulin and/or Arg.sub.2 -(B31-32) human insulin. These mixed crystals are obtained by crystallization from aqueous solution within a narrow pH range (from about 5.5 to about 6.9). The mixed crystals show a specific moderately prolonged profile and are suitable for the treatment of diabetes mellitus.