State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using chemical cross-linking
- 1 October 1987
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 903 (2) , 374-380
- https://doi.org/10.1016/0005-2736(87)90228-8
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using saturation-transfer electron spin resonanceBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Three-dimensional reconstruction of negatively stained crystals of the Ca2+-ATPase from muscle sarcoplasmic reticulumJournal of Molecular Biology, 1986
- Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulumJournal of Molecular Biology, 1985
- The structure of the Ca2+ ATPase as revealed by electron microscopy and image processing of ordered arraysJournal of Ultrastructure Research, 1983
- The application of chemical crosslinking for studies on cell membranes and the identification of surface reportersBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1979
- Cross-linking experiments with the adenosine triphosphatase of sarcoplasmic reticulumBiochemical Journal, 1979
- Cross-linking of the (Ca2+ + Mg2+)-ATPase proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Chemical modification of sarcoplasmic reticulum membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- Cross-linking of the sarcoplasmic reticulum ATPase proteinBiochemical and Biophysical Research Communications, 1976
- The proteins of rabbit skeletal muscle sarcoplasmic reticulumArchives of Biochemistry and Biophysics, 1972