The 240‐kDa subunit of human erythrocyte spectrin binds calmodulin at micromolar calcium concentrations
- 9 June 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 201 (2) , 306-310
- https://doi.org/10.1016/0014-5793(86)80629-9
Abstract
Calmodulin (Human) Spectrin Erythrocyte cytoskeleton Aqueous two-phase partitioningKeywords
This publication has 35 references indexed in Scilit:
- Interaction of calmodulin with the red cell and its membrane skeleton and with spectrinBiochemistry, 1985
- Comparison of spectrin isolated from erythroid and non-erythroid sourcesEuropean Journal of Biochemistry, 1984
- The interaction of calmodulin with human and avian spectrinBiochemical and Biophysical Research Communications, 1984
- Calmodulin binding to human spectrinFEBS Letters, 1984
- The Cytoskeleton of the Red Blood CellPublished by Elsevier ,1983
- Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membraneBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
- Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell typesThe Journal of cell biology, 1982
- Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.Proceedings of the National Academy of Sciences, 1982
- A major calmodulin-binding protein common to various vertebrate tissues.Proceedings of the National Academy of Sciences, 1982
- An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrinCell, 1982