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Erythroid spectrin in miceller detergents

Cell Motility, 2002
AbstractWe have studied the interaction of spectrin, the major protein of the erythrocyte cytoskeleton, with four commonly used detergents at concentrations above their critical miceller concentrations (cmc). Fluorescence spectroscopic studies on the emission intensity, steady state polarization, quenching with acrylamide, and time‐resolved ...
Sibnath, Ray, Abhijit, Chakrabarti
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Interaction of spectrin with hemin disaggregates spectrin associations.

Biochemistry international, 1984
Crude spectrin preparations were extracted from red cell membranes either in dimeric or tetrameric forms and incubated at 4 degrees C with hemin. The mixtures were subjected immediately or after 18 hours to nondenaturing electrophoresis. It was found that immediately after addition of 0.3 mM hemin, the fraction of spectrin complexed with other skeletal
N, Avissar +4 more
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Spectrin-Actin Interactions

1990
The protein spectrin was first reported in 1968 in water-soluble extracts from erythrocyte membranes (Marchesi and Steers, 1968). Although for some time it was believed that spectrin represented a specific erythrocyte adaptation, in recent years spectrin and spectrinlike proteins have been found in a wide range of other cell types (e.g., see Goodman et
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When alpha spectrin null alleles meet low expression alpha spectrin polymorphisms