Clinical Chemistry AACC Online Job Center
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 27: 918-921, 1981;
This Article
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by van Wijk, E. M.
Right arrow Articles by ten Cate, J. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by van Wijk, E. M.
Right arrow Articles by ten Cate, J. W.

Clinical Chemistry, Vol 27, 918-921, Copyright © 1981 by American Association for Clinical Chemistry

Optimization of a mechanized amidolytic factor-X assay; influence of reaction conditions and reagents

EM van Wijk, LH Kahle, M Wiebosch and JW ten Cate

We describe the effect of pH and NaCl concentration on the activation of factor X in plasma by Russell's viper venom and on the amidolytic activity of the activated enzyme towards factor Xa-sensitive chromogenic substrates. An increasing NaCl concentration results in a decrease in the activation rate of factor X by Russell's viper venom, whereas in this step no pH effect is observed. Increasing NaCl concentrations decrease the Km and Vmax for both the factor Xa- sensitive chromogenic substrates, S 2222 and S 2337. Km values were lowest between pH 7.8 and 8.6; Vmax increased with increasing pH. Comparison of NaCl and KCl in the activation step as well as in the amidolytic step shows that the observed effect is specific for Na+, not just an effect of ionic strength. No difference was detected between activation by the crude venom or its purified factor X-activating enzyme. Also, values with the substrates S 2222 or S 2337 were the same in the mechanized amidolytic factor X assay.


The following articles in journals at HighWire Press have cited this article:


Home page
 CLIN APPL THROMB HEMOSTHome page
M. Tobu, O. Iqbal, D. A. Hoppensteadt, C. Shultz, W. Jeske, and J. Fareed
Effects of a Synthetic Factor Xa Inhibitor (JTV-803) on Various Laboratory Tests
Clinical and Applied Thrombosis/Hemostasis, October 1, 2002; 8(4): 325 - 336.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1981 by the American Association for Clinical Chemistry.