Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C
YH Sun, S Tran, EA Norstrøm, B Dahlbäck - Journal of Biological …, 2004 - ASBMB
A Gla domain-mutated protein C variant, QGNSEDY, modified at positions 10–12, 23, 32–
33, and 44, having enhanced affinity for negatively charged phospholipid and increased
anticoagulant potential, was used to elucidate the importance of the interaction between the
Gla domain and the phospholipid for the ability of activated protein C (APC) to inactivate
factor Va (FVa). FVa degradation by wild type (WT)-APC and QGNSEDY-APC yielded
similar fragments on Western blotting; QGNSEDY-APC was, however, considerably more …
33, and 44, having enhanced affinity for negatively charged phospholipid and increased
anticoagulant potential, was used to elucidate the importance of the interaction between the
Gla domain and the phospholipid for the ability of activated protein C (APC) to inactivate
factor Va (FVa). FVa degradation by wild type (WT)-APC and QGNSEDY-APC yielded
similar fragments on Western blotting; QGNSEDY-APC was, however, considerably more …
