Figure 2
Figure 2. Coomassie brilliant blue staining of sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel of purified proteins. Five micrograms of mFVIIa, mFVIIa chimeras, or msEPCR were electrophoresed under reducing or nonreducing conditions. The apparent molecular weights of the marker standard (M) are indicated in kilodaltons. Lanes 1, 3, 5, and 7, nonreducing conditions; lanes 2, 4, 6, and 8, reducing conditions. Arrows point to the full-length (F) (under nonreducing conditions) and the heavy (H) and light (L) chains (under reducing conditions) of each protease. The bracket indicates 2 N-glycosylation variants of the light chain of mFVIIa (or its chimeras), as confirmed by treatment with peptide-N-glycosidase F treatment (data not shown).

Coomassie brilliant blue staining of sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel of purified proteins. Five micrograms of mFVIIa, mFVIIa chimeras, or msEPCR were electrophoresed under reducing or nonreducing conditions. The apparent molecular weights of the marker standard (M) are indicated in kilodaltons. Lanes 1, 3, 5, and 7, nonreducing conditions; lanes 2, 4, 6, and 8, reducing conditions. Arrows point to the full-length (F) (under nonreducing conditions) and the heavy (H) and light (L) chains (under reducing conditions) of each protease. The bracket indicates 2 N-glycosylation variants of the light chain of mFVIIa (or its chimeras), as confirmed by treatment with peptide-N-glycosidase F treatment (data not shown).

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