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    N-TERMINALLY TRUNCATED GLYCOSYLTRANSFERASES
    4.
    发明公开
    N-TERMINALLY TRUNCATED GLYCOSYLTRANSFERASES 审中-公开
    N-末端TRUNKIERTE GLYKOSYLTRANSFERASEN

    公开(公告)号：EP3017041A1

    公开(公告)日：2016-05-11

    申请号：EP14735569.7

    申请日：2014-07-03

    申请人： F.Hoffmann-La Roche AG ,  Roche Diagnostics GmbH

    发明人： CZABANY, Tibor ,  ENGEL, Alfred ,  GREIF, Michael ,  JUNG, Christine ,  LULEY, Christiane ,  MALIK, Sebastian ,  MUELLER, Rainer ,  NIDETZKY, Bernd ,  RIBITSCH, Doris ,  SCHMOELZER, Katharina ,  SCHWAB, Helmut ,  SOBEK, Harald ,  SUPPMANN, Bernhard ,  THOMANN, Marco ,  ZITZENBACHER, Sabine

    IPC分类号： C12N9/10

    摘要： 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.

    摘要翻译： 本公开涉及具有N-末端截短缺失的糖基转移酶变体。 与以前的发现相反，发现包含保守氨基酸基序（“QVWxKDS”）的某些截短与糖基转移酶酶活性相容，特别是在人唾液酸转移酶（hST6Gal-1）中。 因此，所公开的是哺乳动物糖基转移酶的变体，编码它们的核酸，用于重组产生哺乳动物糖基转移酶变体的方法和手段及其用途，特别是作为糖蛋白的部分的聚糖末端受体基团（如免疫球蛋白）的唾液酸化。

    QUANTITATIVE CONTROL OF SIALYLATION
    5.
    发明公开
    QUANTITATIVE CONTROL OF SIALYLATION 有权
    定量管制SIALYIERUNG

    公开(公告)号：EP3004368A1

    公开(公告)日：2016-04-13

    申请号：EP14725130.0

    申请日：2014-05-16

    申请人： F.Hoffmann-La Roche AG ,  Roche Diagnostics GmbH

    发明人： ENGEL, Alfred ,  GREIF, Michael ,  JUNG, Christine ,  MALIK, Sebastian ,  MUELLER, Rainer ,  SOBEK, Harald ,  SUPPMANN, Bernhard ,  THOMANN, Marco

    IPC分类号： C12P21/00 ,  C12P19/18 ,  A61K39/395

    摘要： 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.