Abstract
Heavy sarcoplasmic reticulum (SR) preparations of rabbit skeletal muscle, which are enriched in Ca2+-release vesicles from the terminal cisternae (TC) and [3H]ryanodine receptor density, exhibit 60% of the Ca2+-ATPase activity, 58% of the EP level, and 30% of the steady state Ca2+-loading compared to membrane vesicles from the longitudinal SR. The Ca2+-ATPase of TC SR is solubilized and separated from the Ca2+-ryanodine receptor complex in the insoluble fraction on treatment with the detergent C12E9. However, a 50% decrease in receptor density is observed upon removal of the Ca2+-ATPase, suggesting a significant contribution of this protein to maintaining optimal receptor complex density.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 235-243 |
| Number of pages | 9 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 139 |
| Issue number | 1 |
| DOIs | |
| State | Published - Aug 29 1986 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Solubilization and separation of Ca2+-ATPase from the Ca2+-ryanodine receptor complex. / Pessah, Isaac N; Anderson, Kenneth W.; Casida, John E.
In: Biochemical and Biophysical Research Communications, Vol. 139, No. 1, 29.08.1986, p. 235-243.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solubilization and separation of Ca2+-ATPase from the Ca2+-ryanodine receptor complex
AU - Pessah, Isaac N
AU - Anderson, Kenneth W.
AU - Casida, John E.
PY - 1986/8/29
Y1 - 1986/8/29
N2 - Heavy sarcoplasmic reticulum (SR) preparations of rabbit skeletal muscle, which are enriched in Ca2+-release vesicles from the terminal cisternae (TC) and [3H]ryanodine receptor density, exhibit 60% of the Ca2+-ATPase activity, 58% of the EP level, and 30% of the steady state Ca2+-loading compared to membrane vesicles from the longitudinal SR. The Ca2+-ATPase of TC SR is solubilized and separated from the Ca2+-ryanodine receptor complex in the insoluble fraction on treatment with the detergent C12E9. However, a 50% decrease in receptor density is observed upon removal of the Ca2+-ATPase, suggesting a significant contribution of this protein to maintaining optimal receptor complex density.
AB - Heavy sarcoplasmic reticulum (SR) preparations of rabbit skeletal muscle, which are enriched in Ca2+-release vesicles from the terminal cisternae (TC) and [3H]ryanodine receptor density, exhibit 60% of the Ca2+-ATPase activity, 58% of the EP level, and 30% of the steady state Ca2+-loading compared to membrane vesicles from the longitudinal SR. The Ca2+-ATPase of TC SR is solubilized and separated from the Ca2+-ryanodine receptor complex in the insoluble fraction on treatment with the detergent C12E9. However, a 50% decrease in receptor density is observed upon removal of the Ca2+-ATPase, suggesting a significant contribution of this protein to maintaining optimal receptor complex density.
UR - http://www.scopus.com/inward/record.url?scp=0022557495&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022557495&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(86)80104-8
DO - 10.1016/S0006-291X(86)80104-8
M3 - Article
C2 - 2945551
AN - SCOPUS:0022557495
VL - 139
SP - 235
EP - 243
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -