Clinical Chemistry Link to Randox Laboratories Web Site
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 31: 35-40, 1985;
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 Muszbek, L.
Right arrow Articles by Fesus, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muszbek, L.
Right arrow Articles by Fesus, L.

Clinical Chemistry, Vol 31, 35-40, Copyright © 1985 by American Association for Clinical Chemistry

Kinetic determination of blood coagulation Factor XIII in plasma

L Muszbek, J Polgar and L Fesus

We have designed a new kinetic assay for estimating Factor XIII in plasma. Plasma fibrinogen is removed by treatment with bentonite (colloidal aluminum silicate) before measurement. During the lag phase, Factor XIII is transformed by thrombin and Ca2+ into active transglutaminase (EC 2.3.2.13), which attaches the substrate ethylamine to a glutamine residue in acetylated, dephosphorylated beta-casein. During the reaction, ammonia is released, which can be continuously monitored in an NADPH-dependent indicator reaction catalyzed by glutamate dehydrogenase (EC 1.4.1.4). We determined the optimal concentrations of substrate and activator and found that, to eliminate the clottable fibrinogen from the plasma samples, bentonite treatment was more advantageous than the traditional heat treatment. Results by the method correlate well with those by the most widely used amine incorporation and immunoinhibition assays for Factor XIII. We established a reference interval of 12.1-22.7 U/L; at optimal conditions, the variance of the method was less than 3% within this range. The method has several theoretical and practical advantages over traditional determinations of Factor XIII.


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


Home page
 GutHome page
G D'Argenio, M Calvani, N Della Valle, V Cosenza, G D. Matteo, P Giorgio, S Margarucci, O Petillo, F P Jori, U Galderisi, et al.
Differential expression of multiple transglutaminases in human colon: impaired keratinocyte transglutaminase expression in ulcerative colitis
Gut, April 1, 2005; 54(4): 496 - 502.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Chem.Home page
L. Karpati, B. Penke, E. Katona, I. Balogh, G. Vamosi, and L. Muszbek
A Modified, Optimized Kinetic Photometric Assay for the Determination of Blood Coagulation Factor XIII Activity in Plasma
Clin. Chem., December 1, 2000; 46(12): 1946 - 1955.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
I. Balogh, G. Szoke, L. Karpati, U. Wartiovaara, E. Katona, I. Komaromi, G. Haramura, G. Pfliegler, H. Mikkola, and L. Muszbek
Val34Leu polymorphism of plasma factor XIII: biochemistry and epidemiology in familial thrombophilia
Blood, October 1, 2000; 96(7): 2479 - 2486.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
R. Anwar, L. Gallivan, S. D. Edmonds, and A. F. Markham
Genotype/Phenotype Correlations for Coagulation Factor XIII: Specific Normal Polymorphisms Are Associated With High or Low Factor XIII Specific Activity
Blood, February 1, 1999; 93(3): 897 - 905.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1985 by the American Association for Clinical Chemistry.