PREPARATIVE PURIFICATION PROCESS FOR HUMAN FURIN
    1.
    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

    CPC classification number: C12N9/6454 B01D15/363 C12Y304/21075

    Abstract: 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%.

    Abstract translation: 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。

    Method for the purification of alpha-1 proteinase inhibitor (a1PI)
    5.
    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

    CPC classification number: C07K14/8125

    Abstract: 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.

    Abstract translation: 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)
    6.
    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

    CPC classification number: C07K14/8125

    Abstract: 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.

    Abstract translation: 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
    8.
    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

    CPC classification number: C12N9/6454 B01D15/363 C12Y304/21075

    Abstract: 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%.

    Abstract translation: 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。

Patent Agency Ranking