ABSTRACT: In this work, a novelmeth

ABSTRACT: In this work, a novelmethodwas established to isolate and purify Human plasminogen Kringle 5 (HPK5) as a histidinetagged
fusion protein expressed in Escherichia coli BL21 (DE3). This method consisted of sample extraction using a Ni-chelated
Sepharose Fast-Flow affinity column, ammonium sulfate salting-out and Sephadex G-75 size-exclusion column in turn. The purity
analysis by SDS–PAGE, high-performance size-exclusion and reversed-phase chromatographies showed that the obtained
recombinant fusion HPK5 was homogeneous and its purity was higher than 96%; the activity analysis by chorioallantoic
membrane model of chicken embryos revealed that the purified recombinant HPK5 exhibited an obvious anti-angiogenic activity
under the effective range of 5.0–25.0 μg/mL. Through this procedure, about 19mg purified recombinant fusion HPK5 can be
obtained from 1 L of original fermentation solution. Approximate 32% of the total recombinant fusion HPK5 can be captured
and the total yield was approximately 11%. Copyright © 2013 John Wiley & Sons, Ltd.

Kết quả (Việt) 1:

Abstract: In this work, a novelmethodwas was established to isolate and purify human plasminogen Kringle 5 (HPK5) histidinetagged as a
fusion protein expressed in Escherichia coli BL21 (DE3). This method consists of extraction patterns using a real chelated Ni
Sepharose fast-flow affinity column, ammonium sulfate salting-out and Sephadex G-75 size exclusion column respectively. Purity
by SDS-PAGE analysis, high performance size-exclusion and reverse phase chromatographies showed that the obtained
recombinant fusion HPK5 is homogeneous and its purity is higher than 96 %; analysis works by chorioallantoic
membrane of chicken embryo model revealed that purified recombinant HPK5 exhibited a clear operational anti-angiogenic
lower effective range of 5.0-25.0 microg / mL. Through procedures This, of about 19mg of pure recombinant fusion can HPK5
obtained from 1 L of initial fermentation solution. Approximately 32% of all recombinant fusion HPK5 can be taken
and productivity is all about 11%. Copyright © 2013 John Wiley & Sons, Ltd..

Kết quả (Việt) 2:

ABSTRACT: In this work, a novelmethodwas established to isolate and purify Human plasminogen Kringle 5 (HPK5) as a histidinetagged
Expressed fusion protein in Escherichia coli BL21 (DE3). This consisted of sample extraction method using a Ni-chelated
affinity Sepharose Fast-Flow column, the salting-out with ammonium sulfate and Sephadex G-75 size-exclusion column in turn. The purity
by SDS-PAGE analysis, high-performance size-exclusion and reversed-phase chromatographies showed là thu được
recombinant fusion HPK5 was homogeneous and its purity was 96% higher coal; activity analysis by the chorioallantoic
membrane of chicken ie composed model revealed rằng Obvious purified recombinant HPK5 exhibited an anti-angiogenic activity
under the effective range of 5.0-25.0 microg / mL. Through this procedure, about 19mg can be purified recombinant fusion HPK5
thu được from 1 L of fermentation original solution. Approximate 32% of the total recombinant fusion HPK5 can be captured
and the total yield was approximately 11%. Copyright © 2013 John Wiley & Sons, Ltd..