|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|34188||45008||2016||5 صفحه PDF||ندارد||دانلود رایگان|
• Hollow silica nanospheres (NSs) with Glutatione group (SiO2-GSH) have been prepared.
• SiO2-GSH NSs were applied to purify GST-tagged proteins without any preprocessing.
• The capacity of separated protein barely changed after three times reuse.
• The detection limit is lower than 1.0 × 10−6 mol/L to the target proteins.
• The separated capacity of the SiO2-GSH NSs is as much as 89.9 μmol/g.
A Thiol-functionalized silica hollow nanospheres(denoted as SiO2-SH NSs) were prepared through a hydrothermal route. The SiO2-SH NSs were conjugated with glutathione group (denoted asGSH) to afford SiO2-GSH NSs. The as-prepared SiO2-GSH sample has hollow structure and exhibits an average diameter of about 45 nm and a wall thickness of 10 nm. The SiO2-GSH NSs were used to separate three kinds of GST-tagged proteins (GST-tagged GPX, GST-tagged LOV and GST-tagged 210-6P). These SiO2-GSH NSs exhibit negligible non-specific adsorption, high binding capacity (89.9 μmol/g), the low detection limit (1.0 × 10−6 mol/L) and reuse property, showing great potentiality in purifying GST-tagged proteins.
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Journal: Process Biochemistry - Volume 51, Issue 6, June 2016, Pages 804–808