期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY
卷 126, 期 2, 页码 263-274出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/S1095-6433(00)00197-5
关键词
SERCA-ATPase; smooth muscle; K+-dependence; Ca2+-transport; sea cucumber; uncoupling by ATP; bioenergetics; marine invertebrates
Although several Ca2+-ATPase isoforms have been described in vertebrates, little is known about Ca2+-transport in the muscle of invertebrates. In the microsomal fraction obtained from the sea cucumber (Ludwigothurea grisea) longitudinal body wall smooth muscle, we identified a Ca2+-transport ATPase that is able to transport Ca2+ at the expense of ATP hydrolysis. This enzyme has a high affinity for both. Ca2+ and ATP, an optimum pH around 7.0, and - different from the vertebrate sarcoplasmic reticulum Ca2+-ATPases isoforms so far described - is activated 3- to 5-fold by K+ but not by Li+, at all temperatures, Ca2+ and ATP concentrations tested. Calcium accumulation by the sea cucumber microsomes is inhibited by Mg/ATP concentrations > 1 mM and the accumulated Ca2+ is released to the medium when the ATP concentration is raised from 0.1 to 4.0 mM. (C) 2000 Elsevier Science Inc. All rights reserved.
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