Amino acid sequence of chicken calsequestrin deduced from c DNA: Comparison of calsequestrin and aspartactin
- 1 August 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 170 (3), 1089-1095
- https://doi.org/10.1016/0006-291x(90)90504-g
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Characterization of calsequestrin of avian skeletal muscleJournal of Muscle Research and Cell Motility, 1990
- Calsequestrin, an intracellular calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-binding protein of the extracellular matrixBiochemical and Biophysical Research Communications, 1990
- Amino acid sequence and distribution of mRNA encoding a major skeletal muscle laminin binding protein: an extracellular matrix-associated protein with an unusual COOH-terminal polyaspartate domain.The Journal of cell biology, 1988
- Isolation and characterization of a laminin-binding protein from rat and chick muscle.The Journal of cell biology, 1988
- Characteristics of skeletal muscle calsequestrin: comparison of mammalian, amphibian and avian musclesJournal of Muscle Research and Cell Motility, 1986
- Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle.The Journal of cell biology, 1984
- Ultrastructural localization of calsequestrin in rat skeletal muscle by immunoferritin labeling of ultrathin frozen sections.The Journal of cell biology, 1983
- The distribution of ATPase activities in purified transverse tubular membranesArchives of Biochemistry and Biophysics, 1983
- Characterization of the adenosinetriphosphatase and calsequestrin isolated from sarcoplasmic reticulum of normal and dystrophic chickensCanadian Journal of Biochemistry, 1976
- Interaction of Divalent Cations with the 55,000-Dalton Protein Component of the Sarcoplasmic ReticulumPublished by Elsevier ,1972