The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+ binding protein localized in the lumen of sarcoplasmic reticulum, are the products of two different genes (Fliegel, L., Leberer, E., Green, N.M. and MacLennan, D.H. (1982) FEBS Lett. 242, 297-300), and can be both purified from slow-twitch skeletal muscle of the rabbit (Damiani, E., Volpe, P. and Margreth, A. (1990) J. Muscle Res. Cell Motil. 11, 522-530). Here we show that both CS isoforms coexist in slow-twitch muscle fibers as indicated by indirect immunofluorescent staining of cryosections with affinity-purified antibodies specific for each CS isoform
As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 k...
AbstractLinkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine recep...
A calsequentrin (CS)-like glycoprotein is present in the sarcoplasmic reticulum (SR) of chicken pect...
The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+...
AbstractThe cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capac...
The cardiac and fast-twitch skeletal muscle forms of the Ca2+-binding protein calsequestrin (CS) are...
The time-course of disappearance of slow-cardiac calsequestrin (CS) and that of appearance of the sk...
Calsequestrin was identified in the isolated sarcoplasmic reticulum from skeletal muscle of three ma...
Calsequestrin (CS), the major Ca(2+)-binding protein in the sarcoplasmic reticulum (SR), is thought ...
Calsequestrin was identified in the isolated sarcoplasmic reticulum from skeletal muscle of three ma...
Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lume...
Calsequestrin (CS) is the major Ca2+-binding protein in the sarcoplasmic reticulum (SR) with a dual ...
The relationship between sarcoplasmic reticulum (SR) Ca content and calsequestrin (CSQ) isoforms was...
It is believed that brief, high amplitude Ca2+ transients, as found in fast-twitch muscles, are not ...
AbstractCa2+-handling proteins are important regulators of the excitation–contraction–relaxation cyc...
As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 k...
AbstractLinkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine recep...
A calsequentrin (CS)-like glycoprotein is present in the sarcoplasmic reticulum (SR) of chicken pect...
The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+...
AbstractThe cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capac...
The cardiac and fast-twitch skeletal muscle forms of the Ca2+-binding protein calsequestrin (CS) are...
The time-course of disappearance of slow-cardiac calsequestrin (CS) and that of appearance of the sk...
Calsequestrin was identified in the isolated sarcoplasmic reticulum from skeletal muscle of three ma...
Calsequestrin (CS), the major Ca(2+)-binding protein in the sarcoplasmic reticulum (SR), is thought ...
Calsequestrin was identified in the isolated sarcoplasmic reticulum from skeletal muscle of three ma...
Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lume...
Calsequestrin (CS) is the major Ca2+-binding protein in the sarcoplasmic reticulum (SR) with a dual ...
The relationship between sarcoplasmic reticulum (SR) Ca content and calsequestrin (CSQ) isoforms was...
It is believed that brief, high amplitude Ca2+ transients, as found in fast-twitch muscles, are not ...
AbstractCa2+-handling proteins are important regulators of the excitation–contraction–relaxation cyc...
As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 k...
AbstractLinkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine recep...
A calsequentrin (CS)-like glycoprotein is present in the sarcoplasmic reticulum (SR) of chicken pect...