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首页> 外文期刊>The protein journal >Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.
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Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.

机译:人心脏150 kDa氧调节蛋白(ER伴侣)的分子克隆,序列,功能和结构基础。

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摘要

Apoptosis of heart tissues followed by hypoxia and ischemia leads finally to cardiac insufficiency. The full-length coding sequence of 3301 bp including cDNA(s) of the ER chaperone ORP150, which was specifically induced by hypoxia stress, was cloned from human cardiac infarct. Phylogenetic analyses reveal that human heart ORP150 shares a highly conserved N-terminal ATPase domain among its related family members. Moreover, hydropathic profiling reveals that their ca. 70 N-terminal residues and unique C-terminal halves exhibit similar hydropathy profiles among members. These findings suggest that ORP150 is structurally and functionally well conserved in distant species.
机译:心脏组织的凋亡继之以缺氧和局部缺血最终导致心脏功能不全。从缺氧应激中克隆了3301 bp的全长编码序列,包括ER伴侣蛋白ORP150的cDNA,该序列是由缺氧应激特异性诱导的。系统发育分析表明,人心脏ORP150在其相关家族成员中共有一个高度保守的N端ATPase结构域。此外,亲水性分析揭示了它们的ca。 70个N末端残基和独特的C末端一半在成员中表现出相似的亲水性。这些发现表明,ORP150在远处的物种中在结构和功能上都非常保守。

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