Dissociation of the DNAse‐I · Actin Complex by Formamide
- 1 September 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 110 (2) , 337-341
- https://doi.org/10.1111/j.1432-1033.1980.tb04872.x
Abstract
Rabbit skeletal muscle actin labeled with 125 iodine by an enzymic method is shown to be capable of polymerization and to bind to matrix‐bound pancreatic DNAse I like unlabeled G‐actin. It was used to demonstrate that actin can be released from DNAse‐I–agarose by 35–40% formamide. Actin which was only shortly exposed to this solvent was able to bind again to DNAse I and to form filaments indicating that it has been recovered functionally intact from the affinity matrix.This publication has 7 references indexed in Scilit:
- Isolation of Polymerization‐Competent Cytoplasmic Actin by Affinity Chromatography on Immobilized DNAse I Using Formamide as EluantEuropean Journal of Biochemistry, 1980
- Biochemistry of actomyosin-dependent cell motility (a review).Proceedings of the National Academy of Sciences, 1978
- Depolymerization of F-actin by deoxyribonuclease ICell, 1976
- A Specific 1:1 G‐actin: DNAase I complex formed by the action of DNAase I on F‐actinFEBS Letters, 1975
- Actin Is the Naturally Occurring Inhibitor of Deoxyribonuclease IProceedings of the National Academy of Sciences, 1974
- Purification from Crude Extract by Affinity Chromatography of the Inhibitor of Deoxyribonuclease IEuropean Journal of Biochemistry, 1971
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951