Method for the purification of alpha-1 proteinase inhibitor (a1PI)
    1.
    发明授权
    Method for the purification of alpha-1 proteinase inhibitor (a1PI) 有权
    纯化α-1蛋白酶抑制剂(a1PI)的方法

    公开(公告)号:US07807435B2

    公开(公告)日:2010-10-05

    申请号:US11202349

    申请日:2005-08-11

    IPC分类号: C12N9/99

    CPC分类号: C07K14/8125

    摘要: The present invention relates to a method for the purification of alpha-1 proteinase inhibitor (a1PI) from protein fractions. More specifically, the invention relates to an improved method for the purification of alpha-1 proteinase inhibitor (a1PI), wherein the yield of a1PI can be increased by thawing the starting material and incubating it for several hours before subjecting it to a washing step.

    摘要翻译: 本发明涉及从蛋白质级分纯化α-1蛋白酶抑制剂(a1PI)的方法。 更具体地说,本发明涉及一种纯化α-1蛋白酶抑制剂(a1PI)的改进方法,其中可以通过解冻起始物质并将其孵育数小时,然后使其进行洗涤步骤,从而增加a1PI的产率。

    Method for the purification of alpha-1 proteinase inhibitor (a1PI)
    2.
    发明申请
    Method for the purification of alpha-1 proteinase inhibitor (a1PI) 有权
    纯化α-1蛋白酶抑制剂(a1PI)的方法

    公开(公告)号:US20070037270A1

    公开(公告)日:2007-02-15

    申请号:US11202349

    申请日:2005-08-11

    IPC分类号: C12N9/99

    CPC分类号: C07K14/8125

    摘要: The present invention relates to a method for the purification of alpha-1 proteinase inhibitor (a1PI) from protein fractions. More specifically, the invention relates to an improved method for the purification of alpha-1 proteinase inhibitor (a1PI), wherein the yield of a1PI can be increased by thawing the starting material and incubating it for several hours before subjecting it to a washing step.

    摘要翻译: 本发明涉及从蛋白质级分纯化α-1蛋白酶抑制剂(a1PI)的方法。 更具体地说,本发明涉及一种纯化α-1蛋白酶抑制剂(a1PI)的改进方法,其中可以通过解冻起始物质并将其孵育数小时,然后使其进行洗涤步骤,从而增加a1PI的产率。

    PREPARATIVE PURIFICATION PROCESS FOR HUMAN FURIN
    3.
    发明申请
    PREPARATIVE PURIFICATION PROCESS FOR HUMAN FURIN 有权
    人民币的准备性净化程序

    公开(公告)号:US20090304669A1

    公开(公告)日:2009-12-10

    申请号:US12124390

    申请日:2008-05-21

    IPC分类号: A61K38/48 C12N9/48 A61P43/00

    摘要: Recombinant truncated human furin was expressed in CHO cells and concentrated approximately 50-fold by ultrafiltration and diafiltration. The concentrate was purified by column chromatography on Capto-MMC™ resulting in a 30-50 fold purification factor and a yield of at least 60%. The at least 20% pure preparation obtained after Capto-MMC™ chromatography had already a purification degree allowing on-column maturation of pro-VWF. Then an additional Arginine Sepharose chromatography purification was carried out. This two column process for purification of truncated human furin resulted in an almost pure furin preparation with a specific activity of approximately 290,000 U furin/mg protein and a yield of about 50%.

    摘要翻译: 重组截短的人弗林蛋白酶在CHO细胞中表达,并通过超滤和渗滤浓缩约50倍。 浓缩物通过Capto-MMC TM上的柱色谱纯化,得到30-50倍纯化因子,产率至少为60%。 在Capto-MMC TM色谱上获得的至少20%的纯制剂已经具有允许亲VWF的柱上成熟的纯化程度。 然后进行额外的精氨酸琼脂糖层析纯化。 用于纯化截短的人弗林蛋白酶的这种两柱方法产生几乎纯的弗林蛋白酶制剂,其具有约290,000U弗林蛋白/ mg蛋白质的比活性,约50%的产率。

    Preparative purification process for human furin
    4.
    发明授权
    Preparative purification process for human furin 有权
    人类弗林蛋白酶的制备纯化方法

    公开(公告)号:US08343748B2

    公开(公告)日:2013-01-01

    申请号:US12124390

    申请日:2008-05-21

    IPC分类号: C12N9/14 C07K1/18 C07K1/20

    摘要: Recombinant truncated human furin was expressed in CHO cells and concentrated approximately 50-fold by ultrafiltration and diafiltration. The concentrate was purified by column chromatography on CAPTO MMC™ (mixed cation exchange/hydrophobic interaction gel) resulting in a 30-50 fold purification factor and a yield of at least 60%. The at least 20% pure preparation obtained after CAPTO MMC™ (mixed cation exchange/hydrophobic interaction gel) chromatography had already a purification degree allowing on-column maturation of pro-VWF. Then an additional Arginine Sepharose chromatography purification was carried out. This two column process for purification of truncated human furin resulted in an almost pure furin preparation with a specific activity of approximately 290,000 U furin/mg protein and a yield of about 50%.

    摘要翻译: 重组截短的人弗林蛋白酶在CHO细胞中表达,并通过超滤和渗滤浓缩约50倍。 浓缩物通过CAPTO MMC TM(混合阳离子交换/疏水相互作用凝胶)上的柱色谱纯化,得到30-50倍纯化因子,产率至少为60%。 在CAPTO MMC TM(混合阳离子交换/疏水相互作用凝胶)色谱之后获得的至少20%的纯制剂已经具有允许亲VWF的柱上成熟的纯化度。 然后进行额外的精氨酸琼脂糖层析纯化。 用于纯化截短的人弗林蛋白酶的这种两柱方法产生几乎纯的弗林蛋白酶制剂,其具有约290,000U弗林蛋白/ mg蛋白质的比活性,约50%的产率。

    Stable blood coagulation inhibitor-free factor vii preparation and method for preparing same
    7.
    发明授权
    Stable blood coagulation inhibitor-free factor vii preparation and method for preparing same 有权
    稳定的凝血抑制因子制剂及其制备方法

    公开(公告)号:US06777390B1

    公开(公告)日:2004-08-17

    申请号:US09719945

    申请日:2001-02-20

    IPC分类号: A61K3800

    摘要: Stable pharmaceutical preparations containing blood coagulation Factor VII is disclosed. The pharmaceutical preparations containing blood coagulation Factor VII are free of coagulation inhibitors and are stable over a wide range of environmental conditions. Also provided are blood coagulation Factor VII preparations having a minimum activity of 50 Units/mg of protein that contain less than 5% activated blood coagulation Factor VII (Factor VIIa). The blood coagulation Factor VII containing preparations may also contain other blood coagulation factors and are free from detectable transmissible human pathogens.

    摘要翻译: 公开了含有凝血因子VII的稳定的药物制剂。 含有凝血因子VII的药物制剂不含凝血抑制剂,并且在宽范围的环境条件下是稳定的。 还提供具有最小活性为50单位/ mg蛋白质的含有少于5%的活化凝血因子VII(因子VIIa)的凝血因子Ⅶ制剂。 含有凝血因子Ⅶ的制剂还可含有其他凝血因子,并且不含可检测的可传播的人类病原体。