The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Nov. 01, 2016

Filed:

Dec. 16, 2015
Applicant:

Roche Diagnostics Operations, Inc., Indianapolis, IN (US);

Inventors:

Tibor Czabany, Graz, AT;

Alfred Engel, Weilheim, DE;

Michael Greif, Penzberg, DE;

Christine Jung, Iffeldorf, DE;

Christiane Luley, Hoef-Praebach, AT;

Sebastian Malik, Antdorf, DE;

Rainer Mueller, Penzberg, DE;

Bernd Nidetzky, Graz, AT;

Doris Ribitsch, Graz, AT;

Katharina Schmoelzer, Graz, AT;

Helmut Schwab, Graz, AT;

Harald Sobek, Biberach, DE;

Bernhard Suppmann, Weilheim, DE;

Marco Thomann, Penzberg, DE;

Sabine Zitzenbacher, Graz, AT;

Assignee:

Roche Diagnostics Operations, Inc., Indianapolis, IN (US);

Attorney:
Primary Examiner:
Assistant Examiner:
Int. Cl.
CPC ...
C07K 16/00 (2006.01); C12Q 1/00 (2006.01); C12P 21/00 (2006.01); C12N 9/10 (2006.01);
U.S. Cl.
CPC ...
C12P 21/005 (2013.01); C07K 16/00 (2013.01); C12N 9/1081 (2013.01); C07K 2317/14 (2013.01); C07K 2317/24 (2013.01); C07K 2317/41 (2013.01); C12Y 204/99001 (2013.01);
Abstract

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 β-galactoside-α-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant Δ89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant Δ108 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.


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