Rachel A Anderson

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Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the membrane through associations with transmembrane proteins. A membrane skeletal protein, protein 4.1, is pivotal in the assembly of the membrane skeleton because of its ability to promote associations between spectrin and actin.(More)
Protein 4.1 from human erythrocytes formed a complex with band 3 in inside-out erythrocyte membrane vesicles and with soluble peptides derived from the cytoplasmic domain of band 3. Protein 4.1 labeled metabolically with 32P bound saturably to vesicles depleted of endogenous protein 4.1. The soluble cytoplasmic domain of band 3 (43K) competitively displaced(More)
The cytoskeleton underlying the membrane of erythrocytes is thought to control changes in cell shape such as the diskocyte to the echinocyte. Since the binding of lectins to the transmembrane protein glycophorin blocks the cell shape change, we have proposed that the cytoplasmic end of glycophorin is linked to the cytoskeleton. Here we show that the(More)
Analogues of the human erythroid membrane skeletal component protein 4.1 have been identified in perfused rat tissues and human T and B lymphocyte cell lines. olyclonal antibodies were used which are specific for all domains of protein 4.1, the spectrin-actin-promoting 8-Kd peptide, the membrane-binding 30-Kd domain, and the 50-Kd domain. Antibody(More)
The effects of interactions between drug and skin, drug and vehicle, and vehicle and skin on the overall penetration rate of a drug through the skin may be evaluated by comparison of penetration rates through excised skin and an inert reference membrane such as polyethylene. Dimethyl sulphoxide, dimethyl formamide, ethanol and water increase the(More)
We used a panel of recombinant human apolipoprotein (apo) A-IV truncation mutants, in which pairs of 22-mer alpha-helices were sequentially deleted along the primary sequence, to examine the impact of protein structure and interfacial activity on the ability of apoA-IV to activate cholesterol ester transfer protein. Circular dichroism and fluorescence(More)
The effect of temperature on the permeation of phenolic compounds from aqueous solution through excised human skin has been examined. From a thermodynamic analysis of the data, a mechanism is postulated by which these solutes penetrate through human skin. For the more polar solutes it is suggested that the main resistance to penetration is the lipid(More)