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Tytuł pozycji:

Kinetic characterization of inhibition of human thrombin with DNA aptamers by turbidimetric assay.

Tytuł:
Kinetic characterization of inhibition of human thrombin with DNA aptamers by turbidimetric assay.
Autorzy:
Zavyalova EG; Department of Chemistry, M V Lomonosov Moscow State University, Moscow 119991, Russian Federation. />Protopopova AD
Yaminsky IV
Kopylov AM
Źródło:
Analytical biochemistry [Anal Biochem] 2012 Feb 01; Vol. 421 (1), pp. 234-9. Date of Electronic Publication: 2011 Oct 15.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: <2000- > : San Diego, CA : Elsevier
Original Publication: Orlando Fl : Academic Press
MeSH Terms:
Aptamers, Nucleotide/*pharmacology
Thrombin/*antagonists & inhibitors
Amino Acid Sequence ; Aptamers, Nucleotide/genetics ; Base Sequence ; Chromatography, High Pressure Liquid ; Fibrinogen ; Fibrinopeptide A/genetics ; Fibrinopeptide B/genetics ; Humans ; Hydrolysis ; In Vitro Techniques ; Kinetics ; Microscopy, Atomic Force ; Molecular Sequence Data ; Nephelometry and Turbidimetry/methods ; Thrombin/analysis
Substance Nomenclature:
0 (Aptamers, Nucleotide)
145563-68-4 (thrombin aptamer)
25422-31-5 (Fibrinopeptide A)
36204-23-6 (Fibrinopeptide B)
9001-32-5 (Fibrinogen)
EC 3.4.21.5 (Thrombin)
Entry Date(s):
Date Created: 20111108 Date Completed: 20120524 Latest Revision: 20141120
Update Code:
20240104
DOI:
10.1016/j.ab.2011.10.015
PMID:
22056408
Czasopismo naukowe
A sensitive turbidimetric method for detecting fibrin association was used to study the kinetics of fibrinogen hydrolysis with thrombin. The data were complemented by high-performance liquid chromatography (HPLC) measurements of the peptide products, fibrinopeptides released during hydrolysis. Atomic force microscopy (AFM) data showed that the fibril diameter is the main geometric parameter influencing the turbidity. The turbidimetric assay was validated using thrombin with the standard activity. To study thrombin inhibitors, a kinetic model that allows estimating the inhibition constants and the type of inhibition was proposed. The kinetic model was used to study the inhibitory activity of the two DNA aptamers 15-TBA (thrombin-binding aptamer) and 31-TBA, which bind to thrombin exosites. For the first time, 31-TBA was shown to possess the competitive inhibition type, whereas the shortened aptamer 15-TBA has the noncompetitive inhibition type.
(Copyright © 2011 Elsevier Inc. All rights reserved.)

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