Spectrin, human erythrocyte shapes, and mechanochemical properties
نویسندگان
چکیده
منابع مشابه
Spectrin phosphorylation and shape change of human erythrocyte ghosts
Human erthrocyte membranes in isotonic medium change shape from crenated spheres to biconcave disks and cup-forms when incubated at 37 degrees C in the presence of MgATP (M. P. Sheetz and S. J. Singer, 1977, J. Cell Biol. 73:638-646). The postulated relationship between spectrin phosphorylation and shape change (W. Birchmeier and S. J. Singer, 1977, J. Cell Biol. 73:647-659) is examined in this...
متن کاملIdentification of functional domains of human erythrocyte spectrin.
Isolated human erythrocyte spectrin is a dimer of two unique polypeptide chains. The dimer (alpha beta) undergoes reversible salt- and temperature-dependent association to form (alpha beta)2 tetramers. Spectrin also binds with high affinity to a protein receptor on the cytoplasmic surface of erythrocyte membrane vesicles. By cleavage of spectrin at its cysteine residues with 2-nitro-5-thiocyano...
متن کاملIdentification of proteolytically resistant domains of human erythrocyte spectrin.
Digestion of purified human erthrocyte spectrin with proteolytic enzymes at 0 degrees C results in the production of intermediate-size peptides that resist further cleavage at 0 degrees C. By two-dimensional peptide analysis of these intermediate peptides it has been determined that five unique peptides are produced by tryptic cleavage of the alpha subunit of spectrin (band 1); these have appar...
متن کاملState of Spectrin Phosphorylation Does Not Affect Erythrocyte Shape or Spectrin Binding to Erythrocyte Membranes*
After equilibrating cells with [32P]phosphate there were 3.7 f 0.2 mol of [32P]phosphate/mol of Band 2 subunit; this is the total measured as nonradioactive phosphate in fresh cells (Harris, H. W., Wolfe, L. C., and Lux, S . E. (1978) Fed Roc. 37, 1507). This level can be reduced in intact cells by metabolic depletion, or on purified spectrin by tryptic removal of the terminal phosphorylated pe...
متن کاملState of spectrin phosphorylation does not affect erythrocyte shape or spectrin binding to erythrocyte membranes.
After equilibrating cells with [32P]phosphate there were 3.7 f 0.2 mol of [32P]phosphate/mol of Band 2 subunit; this is the total measured as nonradioactive phosphate in fresh cells (Harris, H. W., Wolfe, L. C., and Lux, S . E. (1978) Fed Roc. 37, 1507). This level can be reduced in intact cells by metabolic depletion, or on purified spectrin by tryptic removal of the terminal phosphorylated pe...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1986
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(86)83644-x