A, schematic presentation of fetuin-A domains.

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A, schematic presentation of fetuin-A domains. A, schematic presentation of fetuin-A domains. Single chain and two-chain forms are shown in the left and right panels, respectively. A, A-chain; CP, connecting peptide; B, B-chain; S–S, disulfide bond. In the right panel, the A-chain and connecting peptide form the heavy chain. The lengths of domains are not to scale. B and C, MALDI-TOF mass spectra of in-gel tryptic digests from heavy chain/acidic (B) and single chain/basic (C) forms of fetuin-A spots. Peptides obtained from the digestion were analyzed by MALDI-TOF-MS. The x axis represents the m/z of ions detected; the y axis represents the relative intensity of the ion in arbitrary units. Enlarged regions of mass spectra represent m/z values from 2000 to 2040 (left) and 2260 to 2340 (right). Peptide peaks at m/z 2016.0 and 2285.2 correspond to amino acids 341–361 (TVVQPSVGAAAGPVVPPCPGR) and 341–363 (TVVQPSVGAAAGPVVPPCPGRIR) of the B-chain of fetuin-A, respectively. Panagiotis M. Karamessinis et al. Mol Cell Proteomics 2008;7:591-599 © 2008 The American Society for Biochemistry and Molecular Biology