Abstract
Proteomic technologies are evolving tools to analyze complex protein patterns that to date have been rarely applied to transfusion medicine. The analysis of prothrombin complex concentrates (PCCs) was used as a model to evaluate to what extent these technologies can detect differences in blood-derived therapeutics beyond that of standard quality control. Three PCCs (two batches each) were individually analyzed for differences in protein content by functional assays, two-dimensional gel electrophoresis, and mass spectrometry. The results were compared to a pool of 72 normal plasma samples. A highly complex protein pattern was found that varied considerably among the three PCCs: 192 spots comprising 40 different proteins were identified. Factor (F) IX activities of the three PCCs were comparable, but their F IX protein contents differed considerably. Many proteins were present in multiple spots (e.g. FII, FX, protein C, vitronectin), indicating a high degree of posttranslational modifications. In comparison with untreated pooled plasma, PCCs displayed several low-molecular-weight variants of proteins that likely constitute potential degradation products. Proteomic technologies allow the identification of potentially modified prot...Continue Reading
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