Boehringer Mannheim Gmbh

Hoffmann-la Roche Inc.

Other

Degussa Aktiengesellschaft

Institut Pasteur

Gesellschaft Fur Biotechnologische Forschung Mbh

University of Stuttgart

Eucodis Bioscience Gmbh

Evonik Degussa Gmbh

F. Hoffmann-la Roche Ag

Universitãt Stuttgart

Wilhelm Tischer

Eva Hoess

Christoph Seidel

Rupert Herrmann

Roberto Falkenstein

Andreas Bommarius

Ralf Mattes

Thomas Meier

Rainer Schmuck

Klaus Reichert

Christoph Syldatk

Bernd Schneidinger

Burkard Wilms

Anja Wiese

Friedrich Popp

Josef Heinle

Ulrich Eicken

Josef Maier

Rolf Deeg

Knut Bartl

Alfred Engel

Philippe Marliere

Reinhard Franze

Hartmut Duefel

Gabriele Pestlin

Michael-Harold Town

Josef Altenbuchner

Josef Burg

Hartmut Ernst Schurig

Manfred Gloger

Hans-Georg Ihlenfeldt

Martin Gerber

Helmut Rehner

Octavian Barzu

Sylvie Pochet

Hellmuth Vetter

Rupert Hermann

Joachim Klein

Peter Stegmuller

Hiroshi Sakamoto

Manfred Wozny

Bernd Hilger

Hans-Dieter Jakubke

Frank Bordusa

Philippe Marlière

Elisabeth Pistotnik

Sibylle Rollinger

Joseph Altenbuchner

Stephan Engelke

Rolf-Joachim Muller

Adelheid Daser

Frank Wedekind

Iris Lein

The invention relates to a mutated trypsin comprising an amino acid substitution both at position K60 and D189, and at least one more amino acid substitution by histidine at position N143 or position E151. Such trypsin mutant has a preferred cleavage site comprising the amino acids Xaa-Xaa-His, wherein Xaais L, Y or F and Xaais R or K. The invention also relates to a man-made polypeptide comprising a target peptide and the above cleavage site as well as to a method of producing C-terminally modified target peptides by using this mutated trypsin.

C-terminal modification of polypeptides

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.

Whole cell catalyst

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. Also disclosed is a nucleic acid encoding the fusion peptide consisting of a first peptide which is an antifusogenic peptide selected from the group of SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and said sequences further consisting of glycine at the C terminal end, N-terminally linked to the second peptide.

Nucleic acids encoding fusion peptides

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

Enzymatic synthesis of deoxyribonucleosides

The present invention refers to conjugates of erythropoietin with poly(ethylene glycol) comprising an erythropoietin glycoprotein having an N-terminal &#x3b1;-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&#x2014;CO&#x2014;(CH)&#x2014;(OCHCH)&#x2014;ORwherein the &#x2014;CO of the poly(ethylene glycol) group forms an amide bond with said N-terminal &#x3b1;-amino group; and wherein R is lower alkyl; x is 2 or 3; and m is from about 450 to about 1350.

Erythropoietin conjugates

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.

Diglycosylated erythropoietin

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.

Process for making antifusogenic fusion peptides that form inclusion bodies

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.

Whole cell catalysts

Immobilization of penicillin G amidase, glutaryl-7-ACA acylase or

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.

Water-soluble proteins modified by saccharides

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.

Use of a derivatized alkaline phosphatase as a standard

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.

Preparation of a water-soluble modified enzyme by covalently bonding an

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.

Process for preparing a carrier useful in immunoassays by deposition of

The present invention provides a stabilized sarcosine oxidase preparation which contains creatineamidinohydrolase covalently bound to a water-soluble polysaccharide.

Stabilized sarcosine oxidase preparation

The present invention provides a process for stabilizing creatine kinase by disulphide modification, wherein creatine kinase is reacted in any desired sequence

Process for stabilizing kinase

Growing community of inventors

Peissenberg, Germany

Wilhelm Tischer