Purification from Starfish Eggs of a Protein that Depolymerizes Actin1
- 1 April 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 89 (4), 1341-1344
- https://doi.org/10.1093/oxfordjournals.jbchem.a133321
Abstract
A protein which is capable of depolymerizing F-actin was purified from an extract of unfertilized starfish eggs by the use of DEAE-cellulose column chromatography and hydroxylapatite column chromatography. This protein has an apparent molecular weight of 17, 000. It inhibited the extent of actin polymerization as well as depolymerizing F-actin rapidly. It was shown that this protein reacts with actin at a molar ratio of 1: 1. The properties of this protein were compared with those of profilin from mammalian tissues.This publication has 4 references indexed in Scilit:
- alpha-Actinin Promotes Polymerization of Actin from ProfilactinEuropean Journal of Biochemistry, 1980
- Isolation and Characterization of Profilactin and Profilin from Calf Thymus and BrainEuropean Journal of Biochemistry, 1980
- Reversal of profilin inhibition of actin polymerization invitro by erythrocyte cytochalasin-binding complexes and cross-linked actin nucleiBiochemical and Biophysical Research Communications, 1980
- Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cellsJournal of Molecular Biology, 1977