Abstract: The current invention reports a polypeptide conjugate, wherein the conjugate comprises a first polypeptide selected from the group of polypeptides comprising SEQ ID NO: 01 and fragments thereof, and a second polypeptide selected from the group of antifusogenic peptides.

Abstract: The present invention relates to a method for the in vitro synthesis of deoxyribonucleosides and enzymes suitable for this method.

Abstract: A whole cell catalyst is described comprising a hydantoinase, a racemase and a carbamoylase. Thus this catalyst is able to degrade hydantoins directly into the amino acids. Additionally, a process for the production of this catalysts and for the production of amino acids is claimed.

Abstract: A process is disclosed for the production of an antifusogenic peptide by producing a fusion peptide of a length of about 14 to 70 amino acids in a prokaryotic host cell, comprising the steps, under such conditions that inclusion bodies of said fusion peptide are formed, of: (a) expressing in said host cell a nucleic acid encoding said fusion peptide consisting of a first peptide which is an antifusogenic peptide of a length of about 10 to 50 amino acids and a second peptide of a length of about 4 to 30 amino acids, said first peptide being N-terminally linked to said second peptide; (b) cultivating said host cell to produce said inclusion bodies; and (c) recovering said antifusogenic peptide from said inclusion bodies, wherein said recovered antifusogenic peptide consists of said fusion peptide or a peptide comprising the antifusogenic peptide of about 10 to 50 amino acids and which is a fragment cleaved from said fusion peptide. Inclusion bodies of the peptides are disclosed.

Abstract: The present invention relates to a method for the in vitro enzymatic synthesis of deoxyribonucleosides and enzymes suitable for this method.

Abstract: The present invention refers to conjugates of erythropoietin with poly(ethylene glycol) comprising an erythropoietin glycoprotein having an N-terminal ?-amino group and having the in vivo biological activity of causing bone marrow cells to increase production of reticulocytes and red blood cells and selected from the group consisting of human erythropoietin and analogs thereof which have the sequence of human erythropoietin modified by the addition of from 1 to 6 glycosylation sites or a rearrangement of at least one glycosylation site; said glycoprotein being covalently linked to one poly(ethylene glycol) group of the formula —CO—(CH2)x—(OCH2CH2)m—OR wherein the —CO of the poly(ethylene glycol) group forms an amide bond with said N-terminal ?-amino group; and wherein R is lower alkyl; x is 2 or 3; and m is from about 450 to about 1350.

Abstract: The instant invention is directed to a rec-hydantoin-racemase from Arthrobacter aurescens DSM 3747. Furthermore, the gene encoding for the racemase and plasmids, vectors and microorganisms comprising this gene are to be protected. Use in a process for the production of amino carboxylic acids or derivatives thereof.

Abstract: This invention is directed to an erythropoietin mutein having in vivo biological activity for causing bone marrow cells to increase production of reticulocytes and red blood cells, in that the mutein is N-glycosylated at Asn38 and Asn83 but not N-glycosylated at Asn24. Such muteins have improved pharmaceutical properties.

Abstract: A process is disclosed for the production of an antifusogenic peptide by producing a fusion peptide of a length of about 14 to 70 amino acids in a prokaryotic host cell, comprising the steps, under such conditions that inclusion bodies of said fusion peptide are formed, of: (a) expressing in said host cell a nucleic acid encoding said fusion peptide consisting of a first peptide which is an antifusogenic peptide of a length of about 10 to 50 amino acids and a second peptide of a length of about 4 to 30 amino acids, said first peptide being N-terminally linked to said second peptide; (b) cultivating said host cell to produce said inclusion bodies; and (c) recovering said antifusogenic peptide from said inclusion bodies, wherein said recovered antifusogenic peptide consists of said fusion peptide or a peptide comprising the antifusogenic peptide of about 10 to 50 amino acids and which is a fragment cleaved from said fusion peptide. Inclusion bodies of the peptides are disclosed.

Abstract: A process is provided for producing an antifusogenic peptide by producing a fusion peptide of from about 14 amino acids up to 70 amino acids in a prokaryotic host cell under conditions in which inclusion bodies are formed. The antifusogenic peptide recovered from the inclusion bodies is a fragment cleaved from the fusion peptide which comprises an antifusogenic peptide.

Abstract: A microorganism is described which is transformed with DNAs which encode a hydantoinnase, a racemase, and a carbamoylase. As a result, the microorganism is able to degrade hydantoins directly to amino acids. A process for the production of the microorganism and a process for producing amino acids with the microorganism is also described.

Abstract: A whole cell catalyst is described comprising a hydantoinase, a racemase and a carbamoylase. Thus this catalyst is able to degrade hydantoins directly into the amino acids.

Abstract: A process is disclosed for the production of an antifusogenic peptide by producing a fusion peptide of a length of about 14 to 70 amino acids in a prokaryotic host cell, comprising the steps, under such conditions that inclusion bodies of said fusion peptide are formed, of: (a) expressing in said host cell a nucleic acid encoding said fusion peptide consisting of a first peptide which is an antifusogenic peptide of a length of about 10 to 50 amino acids and a second peptide of a length of about 4 to 30 amino acids, said first peptide being N-terminally linked to said second peptide; (b) cultivating said host cell to produce said inclusion bodies; and (c) recovering said antifusogenic peptide from said inclusion bodies, wherein said recovered antifusogenic peptide consists of said fusion peptide or a peptide comprising the antifusogenic peptide of about 10 to 50 amino acids and which is a fragment cleaved from said fusion peptide. Inclusion bodies of the peptides are disclosed.

Abstract: This invention is directed to an erythropoietin mutein having in vivo biological activity for causing bone marrow cells to increase production of reticulocytes and red blood cells, in that the mutein is N-glycosylated at Asn38 and Asn83 but not N-glycosylated at Asn24. Such muteins have improved pharmaceutical properties.

Abstract: The present invention refers to conjugates of erythropoietin with poly(ethylene glycol) comprising an erythropoietin glycoprotein having an N-terminal &agr;-amino group and having the in vivo biological activity of causing bone marrow cells to increase production of reticulocytes and red blood cells and selected from the group consisting of human erythropoietin and analogs thereof which have the sequence of human erythropoietin modified by the addition of from 1 to 6 glycosylation sites or a rearrangement of at least one glycosylation site; said glycoprotein being covalently linked to one poly(ethylene glycol) group of the formula

Abstract: An enzyme selected from penicillin-G amidase, glutaryl-7-ACA acylase and D-amino acid oxidase is immobilized by covalent bonding on an aminofunctional organosiloxane polymer carrier to provide an immobilized enzyme having a specific volume activity of at least 100 U/g wet carrier. Preferably, the carrier has an average diameter or 0.01 to 3 mm and is essentially spherical. Covalent bonding is accomplished by activating amino groups on the carrier with a dialdehyde and reacting the activated groups with reactive groups on the enzyme. An amount of enzyme is immobilized to provide a weight ratio of enzyme to carrier of 1 to 300 mg protein per g wet carrier.

Abstract: A water-soluble protein conjugate modified by saccharides is covalently bound to a carbohydrate backbone via a saccharide group. Such protein conjugates modified by saccharides can be produced in a simple way by polymerizing a vinylsaccharide and conjugating in a known way the poly(vinylsaccharide) obtained in this way with the protein, which is preferably an enzyme. The protein conjugates according to the present invention are stable over long time periods at a high enzymatic activity and also in aqueous solution and are thus particularly suitable for use in test kits.

Abstract: Alkaline phosphatase to which is covalently bound a carbohydrate of the general formula ##STR1## wherein n is 0, 1, 2 or 3, A is an acyl radical containing 2 to 5 carbon atoms, R.sup.1 and R.sup.2 are each hydrogen atoms or hydroxyl groups, R.sup.3 is --COOH or --CH.sub.2 OH, R.sup.4 is a hydroxyl group or a --CHOH--CHOH--CH.sub.2 OH or --NH--CO--CH.sub.2 --CH(NH.sub.2)--COOH radical or a complex containing the carbohydrate, is used as a standard for the determination of human alkaline phosphate. Preferred carbohydrates are ovomucoid, chitobiose, chitotriose or N-acetylglucosamine-N-acetylneuraminic acid.

Abstract: A water-soluble polyurethane-modified enzyme is prepared by reaction of an enzyme in aqueous solution with an aqueous solution of a water-soluble polyurethane pre-polymer/bisulfite adduct at a pH greater than 7 to covalently bond the enzyme to the adduct. Preferably, a ratio of enzyme to pre-polymer/bisulfite adduct of from 1:10 to 10:1 is used.

Abstract: The present invention provides a process for the preparation of a specifically bindable protein substance bound to an insoluble carrier material, especially for use in a heterogeneous analysis process, wherein a soluable protein with a molecular weight above about 500,000, which is more hydrophobic than the specifically bindable substance, is coupled to the specifically bindable substance and then the conjugate of reaction component and protein is adsorbed on a hydrophobic solid phase.The present invention also provides a carrier material for use in solid phase immunoassays including a hydrophobic solid phase which is adsorbed on a conjugate of a hydrophobic protein with a molecular weight above about 500,000 and of a specifically bindable protein or protein containing substance.