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Table 1. Results of extraction/excision and affinity experiments for A) serum amyloid Abound to cystatin C (on solid matrix); B) human cystatin C and SAA (on the solid matrix)The complex formation between C-terminal fragments of hCC and SAA was confirmedwith MS experiments. First, we obtained high resolution spectra of the complex(Figure 1A) and then the complex signal was studied by MS/MS analysis (Figure 1B).Fig. 1. ESI-FTICR MS spectrum of complex formed between fragments of hCC(93-120) andSAA(87-105). A) MS spectra of complex in solution; B) MS/MS analysis of complex signal.Our further studies will show which resides are important for interaction of the protein andreveal whole structure of it.AcknowledgmentsThis work is supported by Polish Ministry of Science and Higher Education, grant 1264/H03/2009/37to Dr. Paulina Czaplewska.References1. Grzonka, Z., et al. Acta Biochim Pol. 48, 1-20 (2001).2. Janowski, R., et al. Nat. Struct. Biol. 8, 316-320 (2001).3. Stevens, F.J. Protein Folding Disord. 11, 71-80 (2004).4. Bokarewa, M., et al. J. Rheumatol. 34, 1293-1301 (2007).5. Macht, M., Fiedler, W., Kurzinger, K., Przybylski, M. Biochemistry 35, 15633-15639 (1996).289