Phosphagen kinase evolution. Expression in echinoderms.
Phosphagen kinase evolution. Expression in echinoderms.
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DOI：
10.1111/j.1432-1033.1989.tb15195.x
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发表时间：
1989-12
期刊：
影响因子：
--
通讯作者：
A. Ratto;B. Shapiro;R. Christen
中科院分区：
文献类型：
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作者：
A. Ratto;B. Shapiro;R. Christen
精氨酸激酶和肌酸激酶分别催化ATP与精氨酸和肌酸之间的磷酸基团转移，在细胞能量学中起重要作用。与大多数动物表现出单一磷酸激酶活性（脊索动物中的肌酸激酶和原口动物中的精氨酸激酶）相反，棘皮动物表现出精氨酸激酶和肌酸激酶活性，有时在同一组织中。与肌酸激酶是二聚体（由两个40 kDa的亚基组成）的脊索动物和精氨酸激酶通常是单体（40 kDa）的原口动物不同，棘状动物含有特定的磷酸原激酶：卵中的二聚体精氨酸激酶（由两个42 kDa的亚基组成）和精子中的单体肌酸激酶（145 kDa）。我们已经研究了棘皮动物从现有的五个类（棘，小行星，蛇尾，海参和海百合）的表达，这些特定的磷酸激酶在不同的组织。凝胶过滤用于确定天然酶的分子量。精氨酸激酶或肌酸激酶特异性抗体用于表征SDS/PAGE和转移后精氨酸激酶和肌酸激酶的亚基组成。在所有分析的棘皮动物中，精氨酸激酶总是以约81 kDa的酶的形式出现，该酶由两个42 kDa的亚基组成，肌酸激酶以140-155 kDa的单体酶的形式出现。棘皮动物中发生的两个磷酸激酶具有不同的特异性和特定的分子结构进行了讨论，从发展和进化的角度来看。
Arginine kinase and creatine kinase that catalyze the transfer of a phosphate group between ATP and arginine and creatine, respectively, play an important role in cellular energetics. In contrast to most animals which exhibit a single phosphagen kinase activity (creatine kinase in chordates and arginine kinase in protostomians), echinoderms exhibit both arginine kinase and creatine kinase activities, sometimes in the same tissue. In contrast to chordates in which creatine kinases are dimers (consisting of two subunits of 40 kDa) and protostomians in which arginine kinases are usually monomers (40 kDa), echinoids contain specific phosphagen kinases: a dimeric arginine kinase (consisting of two subunits of 42 kDa) in eggs and a monomeric creatine kinase (145 kDa) in sperm. We have examined echinoderms from the five existing classes (echinoids, asteroids, ophiuroids, holothurians and crinoids) for the expression of these specific phosphagen kinases in different tissues. Gel filtration was used to determine the molecular masses of the native enzymes. Antibodies specific for arginine kinase or for creatine kinase were used to characterize the subunit composition of arginine kinase and creatine kinase after SDS/PAGE and transfer. In all echinoderms analyzed, arginine kinase always occurred as an enzyme of about 81 kDa consisting of two subunits of 42 kDa and creatine kinase as a monomeric enzyme of 140-155 kDa. The occurrence in echinoderms of both phosphagen kinases with distinct specificities and specific molecular structures is discussed from both a developmental and evolutionary point of view.