Extraction of junctional complexes from triad junctions of rabbit skeletal muscle
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry,Physiology
Link
http://link.springer.com/content/pdf/10.1007/BF00121156.pdf
Reference29 articles.
1. BLOCK, B. A., IMAGAWA, T., CAMPBELL, K. P. & Franzini-Armstrong, C. (1988) Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J. Cell Biol. 107, 2587?600.
2. BRADFORD, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein dye-binding. Anal. Biochem. 72, 248?54.
3. BRANDT, N. R., CASWELL, A. H., WEN, S-R. & TALVENHEIMO, J. A. (1990) Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads. J. Memb. Biol. 113, 237?51.
4. BRANDT, N. R., CASWELL, A. H., BRANDT, T., BREW, K. & MELLGREN, R. L. (1992) Mapping of the calpain proteolyses products of the junctional foot protein of the skeletal muscle triad junction. J. Memb. Biol. 127, 35?47.
5. BRANDT, N. R., KAWAMOTO, R. M. & CASWELL, A. H. (1985) Dihydropyridine binding sites on transverse tubules isolated from triads of rabbit skeletal muscles. J. Receptor Res. 5, 155?70.
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