Extraction and Functional Reformation of Thick Filaments in Chemically Skinned Molluscan Catch Muscle Fibers
- 1 February 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 85 (2) , 535-540
- https://doi.org/10.1093/oxfordjournals.jbchem.a132361
Abstract
A method for the almost complete extraction of myosin from smooth muscle fibers of the anterior byssal retractor muscle (ABRM) of Mytilus edulis was developed, and functional refor mation of thick filaments in the fibers was achieved. Complete removal of myosin from the glycerol-extracted ABRM fibers with a solution containing 600 msi KCl, 5 mM MgCl2 and 5 mM ATP was difficult. However, successive treatments of the ABRM fibers with glycerol and saponin made the plasma membrane permeable to Mg˙ATP and myosin. The extraction of myosin completely eliminated the tension induced by the addition of Mg˙ATP. Partial recovery of tension development was observed by irrigation of myosin into fibers from which myosin had been extracted. Similar results were obtained using rabbit myosin instead of ABRM myosin. Addition of heavy meromyosin, on the other hand, had a suppressive effect on the tension development, as is the case in glycerinated rabbit psoas muscle fibers.This publication has 2 references indexed in Scilit:
- Myosin-free Ghosts of Single Fibers and an Attempt to Re-form Myosin Filaments in the Ghost FibersThe Journal of Biochemistry, 1976
- Studies on the structure of myosinJournal of Molecular Biology, 1962