Spectrin tetramer

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Spectrin Tetramer. Such extracts reflect the native oligomeric state of. Spectrin tetramers we expect the centers of the spectrin tetramers to also form a periodic pattern of ring-like structures with a quantitatively simi-lar periodicity. The G46 residue in the. The proportion of dimers and tetramers was determined by gel.

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Spectrin extracted in buffers of low ionic strength 2 spectrin extract was further fractionated on a Sephadex G-200 column M is primarily tetramer at 4C while dimer predominates at with 01 m EDTA pH 75 at 25C. Fluorescence and molecular dynamics studies of free and bound alpha spectrin. Hereditary elliptocytosis HE is a genetically determined disorder of the red cell membrane. Spectrin tetramerization is important for the erythrocyte to maintain its unique shape elasticity and deformability. We used recombinant model proteins to show the importance of one residue G46 in the erythroid α-spectrin junction region that affects spectrin tetramer formation. Spectrin gene fragments encoding the tetramerization domain were amplified Table 1 from preexisting cDNA clones α-spectrin β-spectrin and β H-spectrin or mutated constructs α-spec R22S cloned into pGEX4T-1 sequence verified and expressed in Escherichia coli BL21-CodonPlus DE3-RIPL Agilent Technologies Santa Clara CA using standard methods.

Hereditary elliptocytosis HE is a genetically determined disorder of the red cell membrane.

The proportion of spectrin tetramers and dimers in 4 degrees C low ionic strength extracts of red cell membranes of 9 subjects with 4 different variants of hereditary elliptocytosis HE and 2 subjects with hereditary spherocytosis HS was determined by nondenaturing gel electrophoresis. We used recombinant model proteins to show the importance of one residue G46 in the erythroid alpha-spectrin junction region that affects spectrin tetramer formation. However it is not known whether the same equilibrium exists in the membrane and whether it affects the physical properties of the. The proportion of spectrin tetramers and dimers in 4 degrees C low ionic strength extracts of red cell membranes of 9 subjects with 4 different variants of hereditary elliptocytosis HE and 2 subjects with hereditary spherocytosis HS was determined by nondenaturing gel electrophoresis. Hereditary elliptocytosis HE is a genetically determined disorder of the red cell membrane. Spectrin gene fragments encoding the tetramerization domain were amplified Table 1 from preexisting cDNA clones α-spectrin β-spectrin and β H-spectrin or mutated constructs α-spec R22S cloned into pGEX4T-1 sequence verified and expressed in Escherichia coli BL21-CodonPlus DE3-RIPL Agilent Technologies Santa Clara CA using standard methods.

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Spectrin tetramers we expect the centers of the spectrin tetramers to also form a periodic pattern of ring-like structures with a quantitatively simi-lar periodicity. Spectrin tetramers presumably formed by head-to-head associations of two dimers are twice as long 9. Spectrin gene fragments encoding the tetramerization domain were amplified Table 1 from preexisting cDNA clones α-spectrin β-spectrin and β H-spectrin or mutated constructs α-spec R22S cloned into pGEX4T-1 sequence verified and expressed in Escherichia coli BL21-CodonPlus DE3-RIPL Agilent Technologies Santa Clara CA using standard methods. Highly periodic ring-like structures were indeed ob-served for the C terminus of βII-spectrin in axons Fig. We characterize the tetrame.

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