Segmental Motion and Rotational Diffusion of the Ca2+-translocating Adenosine Triphosphatase of Sarcoplasmic Reticulum, Measured by Time-resolved Phosphorescence Depolarization

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 Jul 1

PMID 6137210

Citations 3

Authors

A Speirs

C H Moore

D H Boxer

P B Garland

Affiliations

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Abstract

We studied the rotational mobility of the Ca2+ + Mg2+-activated ATPase in skeletal-muscle sarcoplasmic-reticulum vesicles, using time-resolved measurements of the depolarization of laser-flash-excited phosphorescence of the extrinsic triplet probe erythrosin. Our results are in general agreement with those of others [Bürkli & Cherry (1981) Biochemistry 20, 138-145] obtained by linear dichroism methods. In addition, we directly observed fast depolarization in the 1-5 microseconds time range that can be attributed to limited motion of part of the protein (segmental motion). Temperature-dependent changes in phosphorescence anisotropy indicated the onset of a conformational change in structure of the Ca2+ + Mg2+-activated ATPase at 11-13 degrees C. We also describe the synthesis of 5-iodoacetamidoerythrosin.

Citing Articles

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Applications of new saturation transfer electron paramagnetic resonance methodology to the rotational dynamics of the Ca-ATPase in sarcoplasmic reticulum membranes.

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Fluorescence energy transfer as an indicator of Ca2+-ATPase interactions in sarcoplasmic reticulum.

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