[HTML][HTML] Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic …
LR Jones, L Zhang, K Sanborn, AO Jorgensen… - Journal of Biological …, 1995 - ASBMB
Previously we identified a protein of apparent M r= 26,000 as the major calsequestrin
binding protein in junctional sarcoplasmic reticulum vesicles isolated from cardiac and
skeletal muscle (Mitchell, RD, Simmerman, HKB, and Jones, LR (1988) J. Biol. Chem. 263,
1376-1381). Here we describe the purification and primary structure of the 26-kDa
calsequestrin binding protein. The protein was purified 164-fold from cardiac microsomes
and shown by immunoblotting to be highly enriched in junctional membrane subfractions. It …
binding protein in junctional sarcoplasmic reticulum vesicles isolated from cardiac and
skeletal muscle (Mitchell, RD, Simmerman, HKB, and Jones, LR (1988) J. Biol. Chem. 263,
1376-1381). Here we describe the purification and primary structure of the 26-kDa
calsequestrin binding protein. The protein was purified 164-fold from cardiac microsomes
and shown by immunoblotting to be highly enriched in junctional membrane subfractions. It …