Isolation of Sarcoplasmic Reticulum Proteins
- Banting and Best Department of Medical Research, Charles H. Best Institute, Toronto, Canada
- Department of Pharmacology, University of Toronto, Toronto, Canada
- G. H. Iles and
- P. Seeman
This extract was created in the absence of an abstract.
Excerpt
The sarcoplasmic reticulum is specialized for binding and release of Ca++ (Ebashi et al., 1969; Martonosi, 1971; Weber, 1966). Because of this specialization, the membrane contains relatively few proteins (Martonosi, 1969; Martonosi and Halpin, 1971; MacLennan, 1970; MacLennan and Wong, 1971; MacLennan et al., 1971), and, as would be expected, many of these proteins interact strongly with Ca++ ion. We are engaged in a program of resolution, characterization, and reconstitution of proteins involved in the Ca++ transport process of sarcoplasmic reticulum (MacLennan, 1970; MacLennan et al., 1971; MacLennan and Wong, 1971). Resolution and characterization have, of necessity, preceded reconstitution, and we have only recently turned our attention to reassembly of the Ca++ transport system from isolated components.
We believe that some seven proteins could be components of the Ca++ transport system. Four of these proteins have been purified to at least 80 % homogeneity; three of the proteins still exist...
