UROCORTIN-III AND USES THEREOF
    125.
    发明公开
    UROCORTIN-III AND USES THEREOF 审中-公开
    乌克兰 - 维也纳共和国

    公开(公告)号:EP1368051A2

    公开(公告)日:2003-12-10

    申请号:EP02753685.3

    申请日:2002-03-15

    摘要: A search of the public human genome database identified a human EST, GenBank accession number AW293249, which has high homology to known pufferfish urocortin sequences. The full length sequence was amplified from human genomic DNA and sequenced. Sequence homology comparisons of the novel sequence with human urocortin I and urocortin II revealed that the sequence encoded a novel human urocortin, which was designated urocortin III (UcnIII). While urocortin III does not have high affinity for either CRF-R1 or CRF-R2, the affinity for CRF-R2 is greater than the affinity for CRF-R1. Urocortin III is capable stimulating cyclic AMP production in cells expressing CRF-R2α or β. Thus, the affinity is high enough that urocortin III could act as a native agonist of CRF-R2. However, it is also likely that urocortin III is a stronger agonist of a yet to be identified receptor.

    摘要翻译: 公众人类基因组数据库的搜索确定了人类EST,GenBank登录号AW293249,其与已知的河豚urocortin序列具有高同源性。 从人类基因组DNA扩增全长序列并进行测序。 新序列与人尿皮质素I和尿皮质素II的序列同源性比较显示,该序列编码新的人类乳皮质素,其命名为尿细胞素III(UcnIII)。 虽然urocortin III对CRF-R1或CRF-R2没有高亲和力,但对CRF-R2的亲和力大于对CRF-R1的亲和力。 Urocortin III能够刺激表达CRF-R2α或bgr的细胞中的环AMP产生。 因此,亲和力足够高,使得尿皮质素III可以作为CRF-R2的天然激动剂。 然而,urocortin III也可能是未被鉴定的受体的更强的激动剂。

    ALCOHOL-FREE WET EXTRACTION OF GLUTEN DOUGH INTO GLIADIN AND GLUTENIN
    128.
    发明授权
    ALCOHOL-FREE WET EXTRACTION OF GLUTEN DOUGH INTO GLIADIN AND GLUTENIN 失效
    在醇溶蛋白和麦谷蛋白面筋面团的无酒精湿法提取

    公开(公告)号:EP0858463B1

    公开(公告)日:2003-09-17

    申请号:EP96922631.5

    申请日:1996-07-01

    IPC分类号: C07K1/30 C07K2/00 C07K14/415

    CPC分类号: C07K14/415

    摘要: An improved alcohol-free method for fractionating gluten into gliadin and glutenin fractions is provided where an acidic dispersion of gluten is formed with a reducing agent (e.g., sodium metabisulfite) operable for breaking disulfide bonds in the gluten protein. Thereafter, the pH of the dispersion is raised to cause glutenin to precipitate while leaving gliadin suspended in the dispersion. The respective fractions can then be separated by decanting or centrifugation. In preferred processing, the dispersion is reacidified prior to separation in order to achieve a higher degree of separation of the glutenin and gliadin.