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Fig. 5 | Malaria Journal

Fig. 5

From: Tryptophan-rich domains of Plasmodium falciparum SURFIN4.2 and Plasmodium vivax PvSTP2 interact with membrane skeleton of red blood cell

Fig. 5

Binding of SURFIN WRD24.2 -His to spectrin. a Immunoblots from the spectrin binding assay. F-actin (positive control), SURFIN WRD24.2 -His, and BSA (negative control) were stripped from spectrin-coated wells, separated by SDS-PAGE, and stained by Coomassie Brilliant Blue (left panel). Immunoblot was performed with anti-His tag antibody and anti-actin antibody (right panel). Expected sizes of SURFIN WRD24.2 -His, actin, spectrin dimer, and BSA were ~46.5, 43, 250, and 66.4 kDa, respectively (indicated by the arrowheads). b The binding affinity of SURFIN WRD24.2 -His, KAHRP320–451-His, and His protein with spectrin. A binding saturation curve was constructed based on values obtained by the ELISA-based assay using serially diluted SURFIN WRD24.2 -His and KAHRP320–451-His. An unrelated His protein was used as the negative control

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