Identification of a calsequestrin-like protein from sea urchin eggs.
作者： J A Oberdorf , D Lebeche , J F Head , B Kaminer
DOI: 10.1016/S0021-9258(18)68714-9
关键词: Biochemistry 、 Sea urchin 、 Calsequestrin 、 Endoplasmic reticulum 、 Arbacia punctulata 、 Amino acid 、 Calcium in biology 、 Egg protein 、 Calcium 、 Biology 、 Cell biology 、 Molecular biology
摘要: Following studies on calcium transport by isolated smooth endoplasmic reticulum from unfertilized sea urchin eggs (Oberdorf, J. A., Head, F., and Kaminer, B. (1986) Cell Biol. 102, 2205-2210) we have purified partially characterized a calsequestrin-like protein this organelle Strongylocentrotus droebachiensis Arbacia punctulata. Muscle calsequestrin sarcoplasmic is well as storage protein. The egg resembles in its behavior purification steps, electrophoretic mobility, blue staining with Stains-all polyacrylamide gels, binding amino acid composition. Purification was attained DEAE-cellulose hydroxyapatite chromatography. Mr of 58,000 the Laemmli gel system reduced to 54,000 under Weber-Osborn (neutral) conditions, thus showing pH dependence although less than occurs muscle calsequestrins. 25% acids are acidic 10% basic. It binds 309 nmol Ca2+/mg protein, within range reported for cardiac calsequestrin. Antigenically, related capable anti-cardiac antibody.
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