Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme.

Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Research Abstract Details 

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Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Abstract Text:

Y Nagata,J Nakamura,T Yamamoto,

Sarcoplasmic reticulum (SR) vesicles were isolated from scallop muscle by the method of Abe et al. (J. Biochem. 112, 822-827, 1992) and their thermolability was examined in the presence and absence of Ca2+. When SR was preincubated at 38 degrees C in the presence of 0.1 mM Ca2+, Ca2+ transport activity decreased as a function of time with a half-inhibition time of about 5 min. Activities of the Ca(2+)-dependent ATPase, phosphoenzyme (EP) formation and E2 to E1 transition were decreased by the heat treatment in parallel with the Ca2+ transport activity. In contrast, when SR was preincubated at 38 degrees C in the presence of 2-5 mM EGTA, all of these activities, except for the Ca2+ transport, were markedly protected from the heat inactivation. The uncoupling between Ca2+ transport and the ATPase reaction did not lead to a rise in the Ca2+ permeability of SR membrane. Plots of the ATPase activity or steady-state level of EP against pCa in the thermal incubation medium revealed a typical sigmoidal curve with a half-inhibition concentration and Hill number of about 0.5 microM and 1.80, respectively. These results suggest that 2 mol of Ca2+ must be removed from the high-affinity Ca2+ binding sites on the ATPase to stabilize the Ca(2+)-ATPase against heat inactivation. The protection from heat inactivation disappeared if SR was preincubated at 38 degrees C after having been solubilized with a nonionic detergent, but returned when the detergent was removed to reconstitute the SR membrane. These results suggest that the protection of ATPase from thermal inactivation in EGTA may require a membrane structure in which the ATPase molecules exist in an appropriate arrangement.

Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Publishing Authors By Initials

Y Nagata,J Nakamura,T Yamamoto,

For similar musculoskeletal system: muscles: muscle, skeletal: sarcoplasmic reticulum research abstracts see: musculoskeletal system: muscles: muscle, skeletal: sarcoplasmic reticulum research

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Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 119

Page Numbers: 1100-5

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1996

Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Keywords Mesh Terms:

KEYWORDS: Sarcoplasmic Reticulum

MESH TERMS: metabolism

Chemical & Substance for Abstract: Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme. Information

Substance Name: Calcium-Transporting ATPases

Registry Number: EC 3.6.1.8

Grant and Affiliation Information for Protection of scallop sarcoplasmic reticulum ATPase from thermal inactivation by removal of calcium from high-affinity binding sites on the enzyme.

AFFILIATION: Faculty of Science Osaka University.

Country: JAPAN

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MEDLINETA: J Biochem

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