Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase
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چکیده
منابع مشابه
Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca -ATPase CHANGES IN CATALYTIC AND TRANSPORT SITES DURING PHOSPHOENZYME HYDROLYSIS*
The structural natures of stable analogues for the ADP-insensitive phosphoenzyme (E2P) of Ca -ATPase formed in sarcoplasmic reticulum vesicles, i.e. the enzymes with bound beryllium fluoride (BeF E2), bound aluminum fluoride (AlF E2), and bound magnesium fluoride (MgF E2), were explored and compared with those of actual E2P formed from Pi without Ca 2 . Changes in trinitrophenyl-AMP fluorescenc...
متن کاملRemarkable stability of solubilized and delipidated sarcoplasmic reticulum Ca2+-ATPase with tightly bound fluoride and magnesium against detergent-induced denaturation.
Conditions were developed in the absence of Ca(2+) for purification, delipidation, and long term stabilization of octaethylene glycol monododecyl ether (C(12)E(8))-solubilized sarcoplasmic reticulum Ca(2+)-ATPase with tightly bound Mg(2+) and F(-), an analog for the phosphoenzyme intermediate without bound Ca(2+). The Ca(2+)-ATPase activity to monitor denaturation was assessed after treatment w...
متن کاملFormation of a stable inactive complex of the sarcoplasmic reticulum calcium ATPase with magnesium, beryllium, and fluoride.
Incubation of leaky or nonionic detergent-solubilized sarcoplasmic reticulum vesicles in solutions containing magnesium, beryllium, and fluoride caused a time-dependent complete inhibition of calcium ATPase activity. The inhibited state persisted through dialysis for 2 days versus EGTA and was reversed within minutes by the presence of 0.5 mM calcium. Calcium-independent ATPase activity was una...
متن کاملFormation of the stable myosin-ADP-aluminum fluoride and myosin-ADP-beryllium fluoride complexes and their analysis using 19F NMR.
The effects of aluminum fluoride and beryllium fluoride on smooth muscle myosin and its subfragments were studied. Mg(2+)-ATPase activity was inhibited in the presence of aluminum fluoride (beryllium fluoride). [3H]ADP bound to heavy meromyosin (HMM) in the presence of aluminum fluoride (beryllium fluoride) and was not dissociated after 3 days of dialysis demonstrating that [3H]ADP was trapped ...
متن کاملRole of divalent cation bound to phosphoenzyme intermediate of sarcoplasmic reticulum ATPase.
Effect of divalent cations bound to the phosphoenzyme intermediate of the ATPase of sarcoplasmic reticulum was investigated at 0 degree C and pH 7.0 using the purified ATPase preparations. Our previous study (Shigekawa, M., Wakabayashi, S., and Nakamura, H. (1983) J. Biol. Chem. 258, 14157-14161) indicated that 1 mol of the ADP-sensitive phosphoenzyme (E1P) formed from CaATP has 3 mol of high a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m313363200