Figure 1.
Figure 1. SDS-PAGE of fibrinogen γ-chain variants. Panel A shows unfractionated (Calbiochem; lane 1), γA/γA (lane 2), and γA/γ′ (lane 3) fibrinogen preparations purified by DE52 anion-exchange chromatography. From top to bottom, bands for theAα, Bβ, and γA chains can be observed. An additional band for the heavier γ′ chain migrates between the γA and Bβ chain in the γA/γ′ preparation as can be observed in lane 3 and 5, and more faintly in lane 1. Panel B shows γA/γA (lane 4) and γA/γ′ (lane 5) fibrinogen purified from one individual.

SDS-PAGE of fibrinogen γ-chain variants. Panel A shows unfractionated (Calbiochem; lane 1), γA/γA (lane 2), and γA/γ′ (lane 3) fibrinogen preparations purified by DE52 anion-exchange chromatography. From top to bottom, bands for theAα, Bβ, and γA chains can be observed. An additional band for the heavier γ′ chain migrates between the γA and Bβ chain in the γA/γ′ preparation as can be observed in lane 3 and 5, and more faintly in lane 1. Panel B shows γA/γA (lane 4) and γA/γ′ (lane 5) fibrinogen purified from one individual.

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