کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9604333 | 43595 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Covalent protein immobilization on glass surfaces: Application to alkaline phosphatase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Covalent protein immobilization on glass surfaces: Application to alkaline phosphatase Covalent protein immobilization on glass surfaces: Application to alkaline phosphatase](/preview/png/9604333.png)
چکیده انگلیسی
Lyophilized alkaline phosphatase (ALPase) was immobilized on aminated glass surfaces using the in vacuo cross-linking process [Simons, B.L., King, M.C., Cyr, T., Hefford, M.A., Kaplan, H., 2002. Zero-length cross-linking of lyophilized proteins. Protein Sci. 11, 1558-1564]. In this procedure, amide bonds were formed between carboxyl groups on the protein and amino groups on the glass surface. After the non-covalently attached enzyme was removed the immobilized ALPase not only retained its activity but could also be used, washed and reused at least six times without significant loss of activity. An average of 1.4 ± 0.6 mg of reusable ALPase per gram of glass fibre was immobilized based on the activity of the soluble equivalent.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Biotechnology - Volume 118, Issue 3, 22 August 2005, Pages 265-269
Journal: Journal of Biotechnology - Volume 118, Issue 3, 22 August 2005, Pages 265-269
نویسندگان
Russell H. Taylor, Sylvie M. Fournier, Brigitte L. Simons, Harvey Kaplan, Mary Alice Hefford,