TY - JOUR
T1 - Solvent perturbation evidence for a two-state system regulated by calcium in sarcoplasmic reticulum ATPase
AU - Fronticelli, Clara
AU - Bucci, Enrico
AU - Shamoo, Adil E.
N1 - Funding Information:
This work was supported in part by grants from NIH HL-13164, DOE DEAS05058EV10329. and NIEHS ES-1248. Computer time and equipment was supported in part by the network of the University of Maryland. based in the Computer Science Center of the College Park Campus.
PY - 1984/5
Y1 - 1984/5
N2 - Perturbation of sarcoplasmic reticulum ATPase with the nonionic detergent C12 E8 is modulated by the amount of free Ca2+ present in the solvent prior to the addition of detergent. CD measurements show that the enzyme exists in solutionin two different conformations that react differently with the detergent. They probably represent the free enzyme, and its complex with Ca2+ On this assumption, titrations with increasing amounts of Ca2+ produced data superimposable on curves obtained measuring Ca2+ bound to sarcoplasmic reticulum vesicles.
AB - Perturbation of sarcoplasmic reticulum ATPase with the nonionic detergent C12 E8 is modulated by the amount of free Ca2+ present in the solvent prior to the addition of detergent. CD measurements show that the enzyme exists in solutionin two different conformations that react differently with the detergent. They probably represent the free enzyme, and its complex with Ca2+ On this assumption, titrations with increasing amounts of Ca2+ produced data superimposable on curves obtained measuring Ca2+ bound to sarcoplasmic reticulum vesicles.
KW - Sarcoplasmic reticulum: A TPase
KW - Solvent perturbation
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U2 - 10.1016/0301-4622(84)87007-6
DO - 10.1016/0301-4622(84)87007-6
M3 - Article
C2 - 6232959
AN - SCOPUS:0021435095
SN - 0301-4622
VL - 19
SP - 255
EP - 258
JO - Biophysical Chemistry
JF - Biophysical Chemistry
IS - 3
ER -