Addition/Correction pubs.acs.org/biochemistry
Correction to Phosphatidylserine-Induced Factor Xa Dimerization and Binding to Factor Va Are Competing Processes in Solution Rinku Majumder, Tilen Koklic, Alireza R. Rezaie, and Barry R. Lentz* Biochemistry 2013, 52 (1), 143−151. DOI: 10.1021/bi301239z
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he corrected legend of Figure 3 appears here. The italicized text clarifies for the reader how molecular mass markers requested by a reviewer were added to gels presented in frames B and C. Figure 3: (A) Native gel electrophoresis of a FXa and FVa mixture in the presence and absence of C6PS. A 5% polyacrylamide gel of a mixture 50 nM FXa and 50 nM FVa in the presence of 400 μM C6PS and 5 mM Ca2+ (lane 1) shows the coexistence of homodimers (FXa·FXa; 90 kDa), heterodimers (FXa·FVa; 224 kDa), and FVa (178 KD), showing that the FXa monomer interacts with both FVa and FXa, which is consistent with the hypothesis that FXa and FVa compete to bind FXa. Lane 2 shows that the same reaction mixture in the absence of C6PS contains only monomers of both FVa and FXa, showing that this competition is regulated by phosphatidylserine (in this case C6PS). Lane 3 shows molecular mass markers. (B) Native gel electrophoresis of FXa and its GLA-EGFNC fragment. The 8% native polyacrylamide gel electrophoresis of FXa and the GLA-EGFNC fragment of FXa in the presence and absence of 400 μM C6PS and 5 mM Ca2+ shows that the GLA-EGFNC fragment does not dimerize in the presence of C6PS and 5 mM Ca2+. (C) The 5% native polyacrylamide gel electrophoresis of 50 nM FVa with and without 50 nM GLA-αEGFNC domain in the presence of 400 μM C6PS and 5 mM Ca2+. Molecular mass markers in f rames B and C were obtained in separate gels run under identical conditions with a range of markers wider than that originally used and lined up with markers in the original gels shown. The results show that the GLA-EGFNC fragment of FXa does not form a complex with FVa.
Received: February 9, 2016
© 2013 American Chemical Society
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DOI: 10.1021/acs.biochem.6b00112 Biochemistry XXXX, XXX, XXX−XXX
