Otoconin-22, the major protein of aragonitic frog otoconia, is a homolog of phospholipase A2.
Otoconin-22, the major protein of aragonitic frog otoconia, is a homolog of phospholipase A2.
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Otoconin-22 是文石蛙耳石的主要蛋白质，是磷脂酶 A2 的同源物。
DOI：
10.1021/bi00070a007
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发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Kretsinger,RH
中科院分区：
文献类型：
--
作者：
Pote,KG;Hauer3rd,CR;Michel,H;Shabanowitz,J;Hunt,DF;Kretsinger,RH
摘要：耳石是脊椎动物前庭系统周围部分形成的蛋白质和无机晶体的复合物。它们增加了细胞外耳锥膜的质量，从而增加了其在线性加速期间的偏转。这增加的质量增加了下面的感觉斑的敏感性。耳石为研究生物矿物质的生长和维持过程中蛋白质和矿物质的相互作用提供了一个很有前途的系统。我们已经纯化了非洲爪蟾文石耳石的主要蛋白，我们称之为otoconin-22，并确定其氨基酸序列和碳水化合物组成。127个氨基酸残基与响尾蛇磷脂酶A2有37%的同源性。我们认为耳锥蛋白-22可能是X. laevis与磷脂酶A2同源并具有相似的三级结构。
Revised Manuscript Received January 4, 1993 abstract: Otoconia are composites of proteins and inorganic crystals formedin the peripheral portion of the vestibular system of vertebrates. They add mass to the extracellular otoconial membrane, thereby increasing its deflection during linear acceleration. This added mass increases thesensitivity of the underlying sensory maculae. Otoconia provide a promising system to decipher the interaction of protein and mineral during the growth and maintenance of biominerals. We have purified the major protein of the aragonitic otoconia of Xenopus laevis, which we call otoconin-22, and determined its amino acid sequence and carbohydrate composition. The 127 residues are 37% identical to the phospholipaseA2 from Crotalus atrox. We propose that otoconin-22 from X. laevis is homologous to phospholipase A2 and has a similar tertiary structure.