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Blood, Vol. 112, Issue 9, 3900-3906, November 1, 2008
Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice
Blood Campanella et al.
112: 3900
Supplemental materials for: Campanella et al
Files in this Data Supplement:
- Figure S1. Direct binding of GAPDH to mouse cytoplasmic domain of band 3 (JPG, 38.2 KB)
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Cloned mouse cdb3 (residues 1–398) was added at a final concentration of 300 nM to a cuvette containing 30 nM rabbit muscle GAPDH (Roche) in a total buffer volume of 1ml (10 mM imidazole acetate, 0.1 mM EDTA, 0.5 mM sodium arsenate, 1 mM sodium phosphate pH 7.0). After 5 min incubation, 0.1 µmol NAD+ and 0.1 µmol glyceraldehyde-3-P were added to start the GAPDH reaction. Kinetic activity of GAPDH was measured by monitoring absorbance at 340 nm. Inhibition of GAPDH activity has been traditionally used to assess the binding of various fragments of cdb3 to GAPDH.5, 6
- Figure S2 (JPG, 139 KB)
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Distribution of LDH (top panels) and PK (lower panels) in dematin headpiece and band 3 knockout mice, and also in erythrocytes containing hypomorphic mutations for ankyrin (nb/nb) and α-spectrin (sph/sph). Staining is the same as in Fig. 6.
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