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Compositional differences in commercial available prothrombin complex concentrates and their activation by tissue factor
Author(s) -
Kahn Daniel,
Hoppensteadt Debra,
Harenberg Job,
Fareed Jawed,
Only Arthur
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.871.1
Subject(s) - thrombin , tissue factor , chemistry , thrombin generation , molecular mass , desorption , composition (language) , mass spectrometry , mole , chromatography , biochemistry , biophysics , coagulation , platelet , enzyme , biology , immunology , medicine , organic chemistry , linguistics , philosophy , adsorption
Prothrombin Complex Concentrates (PCC) are widely used for hemostatic indications. The relative hemostatic efficacy of each concentrate differs due to their composition. We utilized Surface Enhanced Laser Desorption Ionization (SELDI) mass spectrometry to analyze the composition of these agents prior to and after activation with tissue factor. Materials and Method Beriplex®, Cofact®, Octaplex®, Profilnine® and Prothromplex®; along with older lots of Feiba®, Konyne® and Preconativ® were obtained from various vendors. Each of these agents was activated with RecombiPlasTin® and the proteomic profile was obtained in the MW ranges of 0–150 kDa. Results The native PCCs exhibited prominent peaks at 72 kDa, 67 kDa, 59 kDa, 43 kDa and 36 kDa. Upon activation the 72 kDa peak is diminished and a prominent peak is generated in all PCCs at 36–37 kDa. In the MW range of 3 kDa – 20 kDa prominent peaks at varying intensity at 13.9 kDa were noted and a minor peak at 10.5 kDa in the native PCCs. Upon activation a novel peak at 12.6 kDa is generated along with several other fragments below 9 kDa. Conclusions Despite standardization PCCs exhibit wide compositional variations in terms of prothombin content (native) and generated thrombin. Moreover upon activation the consumption of prothrombin and the generation of thrombin also exhibit wide variations as evident by peaks at 36–37 kDa and the generation of the 12.6 kDa peak.