التفاصيل البيبلوغرافية
| العنوان: |
on hydrophobic substrates without exchange |
| المؤلفون: |
Bernhard Von Vacano, Rui Xu, Sabine Hirth, Ines Herzenstiel, Markus Rückel, Thomas Subkowski, Ulf Baus, T. Subkowski, U. Baus |
| المساهمون: |
The Pennsylvania State University CiteSeerX Archives |
| المصدر: |
ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/6d/c9/Anal_Bioanal_Chem_2011_Jun_5_400(7)_2031-2040.tar.gz |
| سنة النشر: |
2011 |
| المجموعة: |
CiteSeerX |
| الوصف: |
The Author(s) 2011. This article is published with open access at Springerlink.com Abstract By combining several surface analytical tools, we show that an adsorbed layer of the protein H*Protein B prevents the adsorption of secondary proteins bovine serum albumin, casein, or collagen at low-salinity conditions and at pH 8. H*Protein B is an industrially producible fusion protein of the hydrophobin family, known for its high interfacial activity. While applications of hydrophobin have been reported to facilitate adhesion of proteins under different pH conditions, careful analysis by quartz-crystal microbalance and ellipsometry prove that no additional adsorption can be found on top of the H*Protein B layer in this study. Surface analysis by X-ray photoelectron spectroscopy and secondary ion mass spectrometry proves that the hydrophobin layer stays intact even after hours of exposure to solutions of the secondary proteins and that no exchange of proteins can be detected. |
| نوع الوثيقة: |
text |
| وصف الملف: |
application/zip |
| اللغة: |
English |
| Relation: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.290.3013 |
| الاتاحة: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.290.3013 |
| Rights: |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
| رقم الانضمام: |
edsbas.EA5E655D |
| قاعدة البيانات: |
BASE |