Patents by Inventor Bernhard Suppmann
Bernhard Suppmann has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Patent number: 9809835Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: GrantFiled: November 24, 2015Date of Patent: November 7, 2017Assignee: Roche Diagnostics Operations, Inc.Inventors: Alfred Engel, Michael Greif, Christine Jung, Sebastian Malik, Rainer Mueller, Harald Sobek, Bernhard Suppmann, Marco Thomann
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Patent number: 9481902Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: GrantFiled: December 16, 2015Date of Patent: November 1, 2016Assignee: Roche Diagnostics Operations, Inc.Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160102333Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: ApplicationFiled: December 16, 2015Publication date: April 14, 2016Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160102298Abstract: The present disclosure is directed to glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations comprising the conserved amino acid motif (“QVWxKDS”) were found to be compatible with glycosyltransferase enzymatic activity, particularly in a human sialyltransferase (hST6Gal-I). Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: ApplicationFiled: December 16, 2015Publication date: April 14, 2016Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160076068Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: ApplicationFiled: November 24, 2015Publication date: March 17, 2016Inventors: Alfred Engel, Michael Greif, Christine Jung, Sebastian Malik, Rainer Mueller, Harald Sobek, Bernhard Suppmann, Marco Thomann
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Patent number: 8236356Abstract: The present invention provides improved media for the cultivation of Clostridium histolyticum and culture supernatants for the biotechnological production of collagenase enzymes. The nutrient media according to the invention comprise one or more peptones from a non-mammalian source, preferably plant-derived peptones. The media can additionally comprise fish gelatin. The invention provides media, culture supernatants comprising Clostridium histolyticum collagenase, and methods to produce said collagenase.Type: GrantFiled: June 4, 2009Date of Patent: August 7, 2012Assignee: Roche Diagnostics Operations, Inc.Inventors: Bernhard Suppmann, Werner Hoelke, Artur Hoffmann, Thomas Marx, Kirsten Sonn, Johann-Peter Thalhofer
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Patent number: 7956167Abstract: The present invention provides a method for purifying Clostridium histolyticum collagenase type I and type II proteins from a complex mixture by subsequently performing a precipitation with ammonium sulfate, hydrophobic interaction chromatography, cation exchange chromatography, and anion chromatography. Conditions are provided which lead to a stabilized, partially purified preparation even after the precipitation step. The method of the invention leads to a quick and efficient removal of other proteolytic activities. The preparations according to the invention provide exceptionally pure and intact collagenase type I and type II proteins which are enzymatically active. The invention also provides blends of the two isolated proteins. The invention further provides the use of the purified collagenase proteins or blends thereof for treating a tissue sample in vitro.Type: GrantFiled: May 29, 2009Date of Patent: June 7, 2011Assignee: Roche Diagnostics Operations, Inc.Inventors: Werner Hoelke, Hellmut Eckstein, Michaela Fischer, Antje Liehre, Bernhard Suppmann, Johann-Peter Thalhofer
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Publication number: 20110070622Abstract: The present invention provides a method for purifying Clostridium histolyticum collagenase type I and type II proteins from a complex mixture by subsequently performing a precipitation with ammonium sulfate, hydrophobic interaction chromatography, cation exchange chromatography, and anion chromatography. Conditions are provided which lead to a stabilized, partially purified preparation even after the precipitation step. The method of the invention leads to a quick and efficient removal of other proteolytic activities. The preparations according to the invention provide exceptionally pure and intact collagenase type I and type II proteins which are enzymatically active. The invention also provides blends of the two isolated proteins. The invention further provides the use of the purified collagenase proteins or blends thereof for treating a tissue sample in vitro.Type: ApplicationFiled: May 29, 2009Publication date: March 24, 2011Inventors: Werner Hoelke, Hellmut Eckstein, Michaela Fischer, Antje Liehre, Bernhard Suppmann, Johann-Peter Thalhofer
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Publication number: 20100086971Abstract: The present invention provides improved media for the cultivation of Clostridium histolyticum and culture supernatants for the biotechnological production of collagenase enzymes. The nutrient media according to the invention comprise one or more peptones from a non-mammalian source, preferably plant-derived peptones. The media can additionally comprise fish gelatin. The invention provides media, culture supernatants comprising Clostridium histolyticum collagenase, and methods to produce said collagenase.Type: ApplicationFiled: June 4, 2009Publication date: April 8, 2010Inventors: Bernhard Suppmann, Werner Hoelke, Artur Hoffmann, Thomas Marx, Kirsten Sonn, Johann-Peter Thalhofer
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Patent number: 7494797Abstract: Truncated terminal deoxynucleotidyl transferase (TdT) derivative from calf thymus, characterized in that the derivative in comparison to the native TdT is N-terminally truncated by up to 161 amino acids and has a 20- to 30-fold higher enzyme activity in solutions containing Co2+ ions, and its recombinant production and use.Type: GrantFiled: April 3, 2003Date of Patent: February 24, 2009Assignee: Roche Diagnostics Operations, Inc.Inventors: Rainer Mueller, Markus Pajatsch, Ingo Curdt, Harald Sobek, Manfred Schmidt, Bernhard Suppmann, Kirsten Sonn, Bernd Schneidinger
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Patent number: 7118901Abstract: A method is provided for the production of a bovine pancreatic protein with a specific desoxyribonuclease activity of at least 6,000 units per mg of protein. Methylotrophic yeast is used as a heterologous host organism. The bovine pancreatic protein is secreted into the growth medium from which it is purified.Type: GrantFiled: December 16, 2003Date of Patent: October 10, 2006Assignee: Roche Diagnostics Operations, Inc.Inventors: Bernhard Suppmann, Johann-Peter Thalhofer, Stephanie Ronning, Helmut Schoen, Rainer Müller
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Patent number: 6902920Abstract: The heterologous expression of the reverse transcriptase from the Avian Myeloblastosis Virus (AMV-RT) in prokaryotic cells and in particular Escherichia coli (E. coli) is described in the present invention. The invention also includes certain measures to simplify the purification of the heterodimeric AMV-RT.Type: GrantFiled: September 21, 2001Date of Patent: June 7, 2005Assignee: Roche Diagnostics Operations, Inc.Inventors: Harald Sobek, Rainer Mueller, Manfred Schmidt, Bruno Frey, Bernhard Suppmann, Rainer Schmuck, Johann-Peter Thalhofer, Peter Pallua, Markus Pajatsch
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Publication number: 20040259197Abstract: A method is provided for the production of a bovine pancreatic protein with a specific desoxyribonuclease activity of at least 6,000 units per mg of protein. Methylotrophic yeast is used as a heterologous host organism. The bovine pancreatic protein is secreted into the growth medium from which it is purified.Type: ApplicationFiled: December 16, 2003Publication date: December 23, 2004Inventors: Bernhard Suppmann, Johann-Peter Thalhofer, Stephanie Ronning, Helmut Schoen, Rainer Muller
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Publication number: 20040248272Abstract: According to the invention, the desoxyribonuclease with increased thermolability is a variant, by way of amino acid substitution, of bovine pancreatic desoxyribonuclease I. The variant protein retains desoxyribonuclease activity. Moreover, the specific desoxyribonuclease activity of the variant of bovine pancreatic desoxyribonuclease I is approximately zero units per mg of protein following heating of the variant of bovine pancreatic desoxyribonuclease I for about 5 min at a temperature below 95° C. In addition, the variant of bovine pancreatic desoxyribonuclease I has no measurable ribonuclease activity.Type: ApplicationFiled: December 19, 2003Publication date: December 9, 2004Inventors: Rainer Muller, Thomas Kirschbaum, Bernhard Suppmann, Helmut Schoen, Richard Engh, Artur Hoffmann, Johann-Peter Thalhofer, Joachim Siedel, Wolf-Dieter Engel
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Publication number: 20040043396Abstract: Truncated terminal deoxynucleotidyl transferase (TdT) derivative from calf thymus, characterized in that the derivative in comparison to the native TdT is N-terminally truncated by up to 161 amino acids and has a 20- to 30-fold higher enzyme activity in solutions containing Co2+ ions, and its recombinant production and use.Type: ApplicationFiled: April 3, 2003Publication date: March 4, 2004Inventors: Rainer Mueller, Markus Pajatsch, Ingo Curdt, Harald Sobek, Manfred Schmidt, Bernhard Suppmann, Kirsten Sonn, Bernd Schneidinger
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Publication number: 20020115147Abstract: The heterologous expression of the reverse transcriptase from the Avian Myeloblastosis Virus (AMV-RT) in prokaryotic cells and in particular Escherichia coli (E. coli) is described in the present invention. The invention also includes certain measures to simplify the purification of the heterodimeric AMV-RT.Type: ApplicationFiled: September 21, 2001Publication date: August 22, 2002Inventors: Harald Sobek, Rainer Mueller, Manfred Schmidt, Bruno Frey, Bernhard Suppmann, Rainer Schmuck, Johann-Peter Thalhofer, Peter Pallua, Markus Pajatsch