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Results: 6

1.
Fig. 2.

Fig. 2. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

Homozygous ld/ld erythrocytes have altered morphology. (Upper) Comparison of whole erythrocytes under a light microscope from wild-type (+/+) and homozygous loop-deleted (ld/ld) mice. (Lower) Comparison of erythrocytes from +/+ and ld/ld mice by using SEM.

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.
2.
Fig. 3.

Fig. 3. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

RBCs from ld/ld mice are osmotically fragile. Erythrocytes from +/+, heterozygous (+/ld), and ld/ld mice were exposed to increasing amounts of saline (x axis). The percent of cells lysed is shown on the y axis.

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.
3.
Fig. 1.

Fig. 1. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

Homologous recombination to delete an 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3. Strategy for targeting the murine Slc4a1 locus (Upper). The amino acid sequence of the β-hairpin loop and the amino acid sequence after the loop deletion (Lower).

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.
4.
Fig. 4.

Fig. 4. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

ld/ld erythrocytes are not deficient in band 3. (a) SDS/PAGE of erythrocyte ghost membranes from +/+, +/ld, and ld/ld mouse blood. (b and c) Western blot of whole RBCs and ghosts from +/+, +/ld, and ld/ld mutant mice. Ctl, human erythrocyte ghosts. Double antibody (anti-band 3 and anti-actin) staining was used.

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.
5.
Fig. 6.

Fig. 6. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

KI-IOVs from ld/ld mice do not bind ankyrin. KI-IOVs (30 μg/ml) were incubated for 3 h on ice with increasing amounts of D3/D4 125I-ankyrin (a) or intact 125I-ankyrin (b). Membranes were pelleted, washed, and assayed in γ counter for radioactive ankyrin (n = 5). The resulting graph is a plot with subtracted heat-denatured controls. Mutant mice KI-IOVs exhibit negligible binding to either the D3/D4 ankyrin fragment of full-length ankyrin.

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.
6.
Fig. 5.

Fig. 5. From: An 11-amino acid ?-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes.

Band 3 retention in membrane skeletons is reduced in ld/ld erythrocytes. SDS/PAGE of whole RBCs extracted with 2% Triton X-100. Bands were quantified with densitometry scanning. One milliliter of packed RBCs was washed three times with PBS and solubilized with 1 ml of 2% Triton X-100 containing 20 μg/ml pepstatin A, 40 μg/ml PMSF, 20 μg/ml leupeptin, 0.5 mM DTT, and 1 mM EDTA, pH = 6.5. The experiment was repeated three times and the average ratio of band 3 to actin from these experiments is shown.

Marko Stefanovic, et al. Proc Natl Acad Sci U S A. 2007 August 28;104(35):13972-13977.

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