American Society of Hematology

Fig. 3.

$Fig. 3. RP-HPLC purification of Gla domain fragments resulting from endoproteinase Asp-N digestion of the protein C light chain originating from plasma of the patient. The peptides were eluted with a linear gradient of acetonitrile, and the effluent was monitored as the absorbance at 214 nm (full line) and 280 nm (broken line). The putative N-terminal Gla fragment(s) of interest absorb at 214 nm, but not at 280 nm, because they are free of Trp and Tyr residues. Peaks fulfilling this criteria are indicated by arrows and numbers. Mass spectra and sequence analysis of each of these fractions showed that the N-terminal Gla domain fragments of the light chain are present in fractions 30 and 31 (see Table 4 and Fig 4).$

RP-HPLC purification of Gla domain fragments resulting from endoproteinase Asp-N digestion of the protein C light chain originating from plasma of the patient. The peptides were eluted with a linear gradient of acetonitrile, and the effluent was monitored as the absorbance at 214 nm (full line) and 280 nm (broken line). The putative N-terminal Gla fragment(s) of interest absorb at 214 nm, but not at 280 nm, because they are free of Trp and Tyr residues. Peaks fulfilling this criteria are indicated by arrows and numbers. Mass spectra and sequence analysis of each of these fractions showed that the N-terminal Gla domain fragments of the light chain are present in fractions 30 and 31 (see Table 4 and Fig 4).

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