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The binding effect of aptamers on thrombin

Paper ID Volume ID Publish Year Pages File Format Full-Text
3879 197 2010 6 PDF Available
Title
The binding effect of aptamers on thrombin
Abstract

Two aptamers that bind separately with exosite I or exosite II of thrombin were studied for better understanding of the binding effect of aptamers on thrombin. CD and intrinsic fluorescence spectra indicated that after binding with aptamers the secondary structure of thrombin seemed unchanged, but the whole conformation of thrombin changed. The binding of aptamers on thrombin also made the catalytic activity of thrombin toward the chromogenic substrate (β-Ala-Gly-Arg-p-nitroanilide diacetate) increased. The present study indicated that the allostery of the two exosites seemed to be independent.

Keywords
Aptamer; Thrombin; Allosteric effect; Chromogenic peptide substrate; Thrombin-binding aptamer; Thrombin conformation
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The binding effect of aptamers on thrombin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 52, Issues 2–3, 15 November 2010, Pages 117–122
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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