Purification and Characterization of Recombinant Human Coagulation Factor XIII A-Chains Expressed in E. coli

1994 ◽  
Vol 5 (2) ◽  
pp. 125-132 ◽  
Author(s):  
T.S. Lai ◽  
M.A. Santiago ◽  
K.E. Achyuthan ◽  
C.S. Greenberg
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Purification And Characterization ◽  
E Coli ◽  
Coagulation Factor Xiii ◽  
Human Coagulation Factor Xiii

Novel polymorphisms and haplotypes in the human coagulation factor XIII A-subunit gene

1996 ◽  
Vol 98 (4) ◽  
pp. 393-395 ◽  
Author(s):  
K. Suzuki ◽  
Jürgen Henke ◽  
Misa Iwata ◽  
Lotte Henke ◽  
Hiroko Tsuji ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Subunit Gene ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Human Coagulation Factor Xiii

Expression of Functional Coagulation Factor XIII in Escherichia coli

1990 ◽  
Vol 63 (02) ◽  
pp. 235-240 ◽  
Author(s):  
P G Board ◽  
K Pierce ◽  
M Coggan
Keyword(s):  
Escherichia Coli ◽  
Factor Xiii ◽  
Blood Clotting ◽  
Coagulation Factor ◽  
E Coli ◽  
Thrombin Cleavage ◽  
Coagulation Factor Xiii ◽  
Clotting Cascade ◽  
Tac Promoter ◽  
A Subunit

SummaryCoagulation factor XIII is a zymogen that can be activated by thrombin cleavage to a transglutaminase that catalyses the formation of covalent crosslinks between fibrin chains in the final stages of the blood clotting cascade. Although circulating factor-XIII is composed of A and B subunits the catalytic activity is a property of the A subunits. In this study we have constructed a plasmid (pKKF13A) that contains a cDNA encoding the A subunit positioned downstream of a tac promoter. Escherichia coli containing this plasmid produce A subunit protein when grown in the presence of IPTG. The cloned A subunit has been partially purified and characterized. Comparison with A subunits purified from plasma showed that the cloned A subunits were of the same size, assembled as dimers, and had the same native electrophoretic mobility. The cloned A subunits expressed transglutaminase activity with putrescine, dansylcadaverine and casein as substrates, and were able to crosslink fibrin in clots formed from A subunit deficient plasma. These studies have demonstrated that functional recombinant factor XIII A subunit can be produced in E. coli and suggest that recombinant factor XIII can potentially provide a safe and inexhaustible supply for therapeutic use.

A highly sensitive fluorometric assay for determination of human coagulation factor XIII in plasma

2007 ◽  
Vol 367 (2) ◽  
pp. 152-158 ◽  
Author(s):  
Kai Oertel ◽  
Andreas Hunfeld ◽  
Edgar Specker ◽  
Christine Reiff ◽  
Rainer Seitz ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Fluorometric Assay ◽  
Coagulation Factor Xiii ◽  
Highly Sensitive ◽  
Human Coagulation Factor Xiii

In VitroSecretion Deficits are Common Among Human Coagulation Factor XIII Subunit B Missense Mutants: Correlations with Patient Phenotypes and Molecular Models

2013 ◽  
Vol 34 (11) ◽  
pp. 1490-1500 ◽  
Author(s):  
Arijit Biswas ◽  
Anne Thomas ◽  
Carville G. Bevans ◽  
Vytautas Ivaskevicius ◽  
Johannes Oldenburg
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Molecular Models ◽  
Coagulation Factor Xiii ◽  
Subunit B ◽  
Human Coagulation Factor Xiii
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