مقاله Highly efficient purification of 6×histidine-tagged recombinant protein-A by MnFe2O4@NH2@2AB-Ni as a novel and highly stable magnetic nanoparticles

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فایل ورد مقاله Highly efficient purification of 6×histidine-tagged recombinant protein-A by MnFe2O4@NH2@2AB-Ni as a novel and highly stable magnetic nanoparticles  کاملا فرمت بندی و تنظیم شده در استاندارد دانشگاه  و مراکز دولتی می باشد.

توجه : در صورت  مشاهده  بهم ریختگی احتمالی در متون زیر ،دلیل ان کپی کردن این مطالب از داخل فایل ورد می باشد و در فایل اصلی مقاله Highly efficient purification of 6×histidine-tagged recombinant protein-A by MnFe2O4@NH2@2AB-Ni as a novel and highly stable magnetic nanoparticles،به هیچ وجه بهم ریختگی وجود ندارد

بخشی از متن مقاله Highly efficient purification of 6×histidine-tagged recombinant protein-A by MnFe2O4@NH2@2AB-Ni as a novel and highly stable magnetic nanoparticles :

تعداد صفحات:۵
چکیده:

In this study we have developed a simple, cheap, and rapid method for purification of 6×histidine-taggedrecombinant proteins with high yields. The new immobilized metal ion affinity adsorbent was synthesized followingco-precipitation method in order to synthesis of superparamagnetic manganes ferrit nanoparticles, and subsequentlycoated with 3-aminopropyltriethoxysilane (APTES) through a silanization reaction. Manganese ferrite nanoparticlesafforded bidentate ligands as a result of reaction between isatoic anhydride and amino-functionalized MnFe2O4. Thestable surface functionalized nanoparticles were further linked with Ni2+ for purification of 6× His-tagged proteins. Thenanoparticles were approximately 75 nm in size and were stable and had negligible non-specific binding for protein.