Figure 7.
Figure 7. Posttranslational modifications in bovine V and pseutarin C nonenzymatic subunit. The disulphide pattern in bovine FVa (A) and pseutarin C nonenzymatic subunit (B) are shown. The α, β, and γ loops are labeled according to Xue et al.43 Free cysteines are shown as “- SH.” Both bovine FV and pseutarin C nonenzymatic subunit are glycosylated. The potential N-glycosylation sites in bovine FV (C) and pseutarin C nonenzymatic subunit (D) are shown. ○ represents potential novel N-glycosylation sites in pseutarin C nonenzymatic subunit compared with bovine FV; •, potential N-glycosylation sites (C) the conserved potential N-glycosylation sites (D).

Posttranslational modifications in bovine V and pseutarin C nonenzymatic subunit. The disulphide pattern in bovine FVa (A) and pseutarin C nonenzymatic subunit (B) are shown. The α, β, and γ loops are labeled according to Xue et al.43  Free cysteines are shown as “- SH.” Both bovine FV and pseutarin C nonenzymatic subunit are glycosylated. The potential N-glycosylation sites in bovine FV (C) and pseutarin C nonenzymatic subunit (D) are shown. ○ represents potential novel N-glycosylation sites in pseutarin C nonenzymatic subunit compared with bovine FV; •, potential N-glycosylation sites (C) the conserved potential N-glycosylation sites (D).

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