The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure.
- 1 September 1982
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 94 (3) , 565-573
- https://doi.org/10.1083/jcb.94.3.565
Abstract
There is an 85,000-dalton protein, called 85K [kilodalton] amorphin, associated with the Z-band of chicken pectoralis muscle myofibrils. This protein was purified and isolated. It is not a structural component of the Z-filaments, since it can be extracted completely without extraction of the Z-filaments. Extraction of 85K amorphin results in loss of specific staining of the Z-band with fluorescence specific anti-85K amorphin. Actinin is the structural component of the Z-filaments, since extraction of .alpha.-actinin is accompanied by loss of the Z-filament structure.This publication has 35 references indexed in Scilit:
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- The existence of an insoluble Z disc scaffold in chicken skeletal muscleCell, 1978
- Fine structure of the vertebrate Z-discJournal of Molecular Biology, 1977
- The myosin filament: III. C-proteinJournal of Molecular Biology, 1975
- Purification and properties of the isolated honeybee Z-discJournal of Molecular Biology, 1974
- THE STRUCTURE OF A SIMPLE Z LINEThe Journal of cell biology, 1973
- The effect of tilting ultrathin sections on the image of the Z-disc of skeletal muscleCellular and Molecular Life Sciences, 1973
- Studies on purified α-actinin: II. Electron microscopic studies on the competitive binding of α-actinin and tropomyosin to Z-line extracted myofibrilsJournal of Molecular Biology, 1972
- Studies on purified α-actinin: I. Effect of temperature and tropomyosin on the α-actinin/F-actin interactionJournal of Molecular Biology, 1972
- The myosin filamentJournal of Molecular Biology, 1967