Growth medium for clostridium histolyticum without ingredient of mammalian source
    3.
    发明专利
    Growth medium for clostridium histolyticum without ingredient of mammalian source 有权
    不含马鞭草源成分的胶原蛋白的生长培养基

    公开(公告)号:JP2009297028A

    公开(公告)日:2009-12-24

    申请号:JP2009139667

    申请日:2009-06-10

    CPC classification number: C12N1/20 C12N9/52

    Abstract: PROBLEM TO BE SOLVED: To provide an improved medium for culturing Clostridium histolyticum and culture supernatants for biotechnologically producing collagenase enzymes.
    SOLUTION: The culture media contain water, fish gelatin and peptones derived from a non-mammalian source. The media preferably contain peptones derived from plants as a non-mammalian source. The media also may contain two or more different peptones. Disclosed are sterilized compositions comprising the media, a culture supernatant containing the collagenase of Clostridium histolyticum, a method for producing the culture supernatant, and a method for producing the collagenase.
    COPYRIGHT: (C)2010,JPO&INPIT

    Abstract translation: 要解决的问题:提供用于培养溶组织梭菌和用于生物技术生产胶原酶的培养上清液的改进培养基。 解决方案:培养基含有源自非哺乳动物来源的水,鱼明胶和胨。 培养基优选含有源自植物的胨作为非哺乳动物来源。 媒体也可能含有两种或更多种不同的蛋白胨。 公开了包含培养基的灭菌组合物,含有溶组织梭菌胶原酶的培养上清液,培养上清液的制备方法和胶原酶的制备方法。 版权所有(C)2010,JPO&INPIT

    Improved purification of collagenase from clostridium histolyticum liquid culture
    5.
    发明专利
    Improved purification of collagenase from clostridium histolyticum liquid culture 有权
    从胶原蛋白液体培养物中提取胶原蛋白的改进

    公开(公告)号:JP2009291195A

    公开(公告)日:2009-12-17

    申请号:JP2009133447

    申请日:2009-06-02

    CPC classification number: C12N9/52 C07K14/33

    Abstract: PROBLEM TO BE SOLVED: To provide a method for purifying Clostridium histolyticum collagenase type I and type II proteins from a complex mixture. SOLUTION: The method for purifying Clostridium histolyticum collagenase includes carrying out the purification by performing precipitation with ammonium sulfate, hydrophobic interaction chromatography, cation exchange chromatography, and anion chromatography. Conditions are provided which lead to a stabilized partially purified preparation and the precipitation step. The preparations provide exceptionally pure and intact collagenase type I and type II proteins which are enzymatically active. The blends of the two isolated proteins are provided. The use of the purified collagenase proteins or blends thereof for treating a tissue sample in vitro are also provided. COPYRIGHT: (C)2010,JPO&INPIT

    Abstract translation: 待解决的问题:提供从复合混合物中纯化溶组织梭状芽胞杆菌胶原酶I型和II型蛋白的方法。 解决方案:用于纯化溶组织梭菌胶原酶的方法包括通过用硫酸铵进行沉淀,疏水相互作用层析,阳离子交换层析和阴离子色谱法进行纯化。 提供了导致稳定的部分纯化制剂和沉淀步骤的条件。 该制剂提供非常纯的和完整的胶原酶I型和II型蛋白质,其具有酶促活性。 提供了两种分离的蛋白质的共混物。 还提供了纯化的胶原酶蛋白或其混合物用于在体外处理组织样品的用途。 版权所有(C)2010,JPO&INPIT

    QUANTITATIVE CONTROL OF SIALYLATION

    公开(公告)号:CA2908407C

    公开(公告)日:2022-06-14

    申请号:CA2908407

    申请日:2014-05-16

    Abstract: 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.

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