Localization of E1–E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling

1986 ◽  
Vol 93 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Jens P. Andersen ◽  
Bente Vilsen ◽  
John H. Collins ◽  
Peter L. Jørgensen
Biochemistry ◽  
1974 ◽  
Vol 13 (16) ◽  
pp. 3298-3306 ◽  
Author(s):  
Giuseppe Inesi ◽  
Donald Scales

1988 ◽  
Vol 173 (2) ◽  
pp. 361-367 ◽  
Author(s):  
Katalin TOROK ◽  
Brian J. TRINNAMAN ◽  
N. Michael GREEN

1986 ◽  
Vol 237 (1) ◽  
pp. 197-206 ◽  
Author(s):  
R J Froud ◽  
A G Lee

We have studied the fluorescence of the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum labelled with fluorescein isothiocyanate. The change in intensity of fluorescein fluorescence caused by addition of Ca2+ to the labelled ATPase can be interpreted in terms of a two-conformation model for the ATPase, one conformation (E1) having a high affinity for Ca2+, the other (E2) a low affinity. Effects of Ca2+ as a function of pH allow an estimate of the effect of pH on the E1/E2 ratio, consistent with kinetic studies. A model is presented for binding of Ca2+ to the ATPase as a function of pH that is consistent both with the data on the E1/E2 equilibrium and with literature data on Ca2+ binding.


1985 ◽  
Vol 128 (3) ◽  
pp. 1159-1163 ◽  
Author(s):  
J.L.R. Arrondo ◽  
M.A. Urbaneja ◽  
F.M. Goñi ◽  
J.M. Macarulla ◽  
G. Sarzala

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