Solubilization of Native Actin Monomers from Human Erythrocyte Membranes
Open Access
- 1 January 1986
- journal article
- research article
- Published by CSIRO Publishing in Australian Journal of Biological Sciences
- Vol. 39 (2) , 117-124
- https://doi.org/10.1071/bi9860117
Abstract
Up to 50% of the actin in erythrocyte membranes can be solubilized at low ionic strength in a form capable of inhibiting DNAse I, in the presence of 0.4 mM and ATP and 0.05 mM calcium. In the absence of calcium and ATP, actin is released but is apparently rapidly denatured. Solubilization of G-actin increases with temperature up to 37.degree. C. At higher temperatures, actin is released rapidly but quickly loses it''s ability to inhibit DNAse I.Keywords
This publication has 12 references indexed in Scilit:
- Structural and dynamic states of actin in the erythrocyteThe Journal of cell biology, 1983
- Investigation of the actin-deoxyribonuclease I interaction using a pyrene-conjugated actin derivativeBiochemistry, 1982
- 2,3-Diphosphoglycerate and ATP dissociate erythrocyte membrane skeletons.Journal of Biological Chemistry, 1980
- In vitro formation of a complex between cytoskeletal proteins of the human erythrocyteNature, 1979
- Comparison of structure and function of human erythrocyte and human muscle actin.Proceedings of the National Academy of Sciences, 1979
- Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease ICell, 1978
- Physical‐chemical studies of spectrinJournal of Supramolecular Structure, 1978
- Structural study of spectrin from human erythrocyte membranesBiochemistry, 1977
- The removal of the bound ADP of F-actinJournal of Molecular Biology, 1966
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951