Results 151 to 160 of about 21,720 (189)
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Brain spectrin(240/235A): A novel astrocyte specific spectrin isoform
Brain Research Bulletin, 1989We have previously demonstrated the existence of two distinct isoforms of spectrin in mammalian brain (23). Brain spectrin(240/235) is found primarily in neuronal axons and presynaptic terminals, and brain spectrin(240/235E) is located in neuronal cell bodies, dendrites and postsynaptic terminals, and oligodendrocytes.
S R, Goodman +4 more
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[8B7 spectrin--a new member of spectrin family].
Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae, 2007To analyze the nature of the protein encoded by 8B7cDNA (1 835 bp) and to examine the localization of the protein in cells.The nature of the protein was analyzed using Blastn, Blastp, and TMpred. Expressions of 8B7 mRNA in tissues and cells were examined by Northern blotting.
Rong, Liu +6 more
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Cell, 1985
Analysis of the turnover of unassembled proteins during the assembly of the erythroid membrane skeleton has revealed that alpha- and beta-spectrin, two structurally related, high molecular weight proteins, are degraded in a selective manner by two distinct intracellular pathways. Unassembled alpha-spectrin (t1/2 approximately equal to 2 hr) is degraded
C M, Woods, E, Lazarides
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Analysis of the turnover of unassembled proteins during the assembly of the erythroid membrane skeleton has revealed that alpha- and beta-spectrin, two structurally related, high molecular weight proteins, are degraded in a selective manner by two distinct intracellular pathways. Unassembled alpha-spectrin (t1/2 approximately equal to 2 hr) is degraded
C M, Woods, E, Lazarides
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Binding of an 80 000 dalton trypsin fragment of spectrin to intact spectrin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982A specific and saturable interaction of an 80 000 dalton tryptic fragment of spectrin with intact spectrin has been detected. When spectrin was incubated with 125I-labelled 80 kDa fragment at 37 degrees C in the presence of 0.1 M NaCl, acrylamide gradient gel electrophoresis showed the presence of bands in addition to the usual spectrin dimer and ...
M, Hanspal, G B, Ralston
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A Conformational Study of Human Spectrin
European Journal of Biochemistry, 1980Urea denaturation profiles of spectrin dimer, measured by circular dichroism in the regions of the peptide and aromatic Cotton effects, reflect the existence of several independently unfolding domains, as well as the presence of flexible, non‐globular structure.
R, Calvert, E, Ungewickell, W, Gratzer
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Interaction of spectrin with hemin disaggregates spectrin associations.
Biochemistry international, 1984Crude 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 extractability in blood storage
Transfusion, 1981The extractability of spectrin from red blood cell membranes was measured both by dialysis against 1 mM EDTA for 44 hours and by incubation with 1 mM EDTA for 60 minutes. We confirmed that the extractability of spectrin is somewhat impaired when membranes are prepared from metabolically depleted erythrocytes, but the extent of impairment was ...
E, Beutler, D, Villacorte
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Protein Expression and Purification, 2008
It was previously shown that ankyrins play a crucial role in the membrane skeleton arrangement. Purifying ankyrinR obtained from erythrocytes is a time-consuming process. Therefore, cloned and bacterially expressed ankyrinR-spectrin-binding domain (AnkSBD) is a demanded tool for studying spectrin-ankyrin interactions.
Adam, Kolondra +3 more
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It was previously shown that ankyrins play a crucial role in the membrane skeleton arrangement. Purifying ankyrinR obtained from erythrocytes is a time-consuming process. Therefore, cloned and bacterially expressed ankyrinR-spectrin-binding domain (AnkSBD) is a demanded tool for studying spectrin-ankyrin interactions.
Adam, Kolondra +3 more
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1996
Abstract Spectrin belongs to the family of actin-binding proteins. It is a structural protein associated with the cytoplasmic surface of the plasma membrane. It is composed of an a- and {3-subunit and was first defined in red blood cells. ft has been found in most metazoans including vertebrates and higher plants.
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Abstract Spectrin belongs to the family of actin-binding proteins. It is a structural protein associated with the cytoplasmic surface of the plasma membrane. It is composed of an a- and {3-subunit and was first defined in red blood cells. ft has been found in most metazoans including vertebrates and higher plants.
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