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10.1016/j.bbagen.2013.02.013 http://scihub22266oqcxt.onion/10.1016/j.bbagen.2013.02.013 C3674504!3674504!23434438     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochim+Biophys+Acta 2013 ; 1830 (6): 3489-96 Nephropedia Template TP {{tp|p=23434438|t=2013. Disulfide reduction abolishes tissue factor cofactor function |pdf=|usr=}}{{23434438}} gab.com Text Disulfide reduction abolishes tissue factor cofactor function JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=23434438 #FOAvip Background: Tissue factor (TF), an in vivo initiator of blood coagulation, is a transmembrane protein and has two disulfides in the extracellular domain. The integrity of one cysteine pair, Cys186?Cys209, has been hypothesized to be essential for an allosteric ?decryption? phenomenon, presumably regulating TF procoagulant function, which has been the subject of a lengthy debate. The conclusions of published studies on this subject are based on indirect evidences obtained by the use of reagents with potentially oxidizing/reducing properties. Methods: The status of disulfides in recombinant TF1?263 and natural placental TF in their non-reduced native and reduced forms was determined by mass-spectrometry. Functional assays were performed to assess TF cofactor function. Results: In native proteins, all four cysteines of the extracellular domain of TF are oxidized. Reduced TF retains factor VIIa binding capacity but completely loses the cofactor function. Conclusion: The reduction of TF disulfides (with or without alkylation) eliminates TF regulation of factor VIIa catalytic function in both membrane dependent FX activation and membrane independent synthetic substrate hydrolysis. General significance: Results of this study advance our knowledge on TF structure/function relationships. Twit Text FOAVip Disulfide reduction abolishes tissue factor cofactor function ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=23434438 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23434438 #FOAvip English Wikipedia <ref>{{Cite pmid|23434438}}</ref> Disulfide reduction abolishes tissue factor cofactor function #MMPMID23434438 Krudysz-Amblo J; Jennings ME; Knight T; Matthews DE; Mann KG; Butenas S Biochim Biophys Acta 2013[Jun]; 1830 (6): 3489-96 PMID23434438show ga Background: Tissue factor (TF), an in vivo initiator of blood coagulation, is a transmembrane protein and has two disulfides in the extracellular domain. The integrity of one cysteine pair, Cys186?Cys209, has been hypothesized to be essential for an allosteric ?decryption? phenomenon, presumably regulating TF procoagulant function, which has been the subject of a lengthy debate. The conclusions of published studies on this subject are based on indirect evidences obtained by the use of reagents with potentially oxidizing/reducing properties. Methods: The status of disulfides in recombinant TF1?263 and natural placental TF in their non-reduced native and reduced forms was determined by mass-spectrometry. Functional assays were performed to assess TF cofactor function. Results: In native proteins, all four cysteines of the extracellular domain of TF are oxidized. Reduced TF retains factor VIIa binding capacity but completely loses the cofactor function. Conclusion: The reduction of TF disulfides (with or without alkylation) eliminates TF regulation of factor VIIa catalytic function in both membrane dependent FX activation and membrane independent synthetic substrate hydrolysis. General significance: Results of this study advance our knowledge on TF structure/function relationships. äDisulfide reduction abolishes tissue factor cofactor function (epmc).pdf DeepDyve Pubget Overpricing