CMP-N-acetylneuraminic acid hydroxylase is exclusively inactive in humans
CMP-N-acetylneuraminic acid hydroxylase is exclusively inactive in humans
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DOI：
10.1006/bbrc.1998.8946
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发表时间：
1998-07-20
影响因子：
3.1
通讯作者：
Suzuki, A
中科院分区：
文献类型：
--
作者：
Irie, A;Suzuki, A
我们克隆了小鼠和人 CMP-N-乙酰神经氨酸 (CMP-NeuAc) 羟化酶的 cDNA，并表明人 CMP-NeuAc 羟化酶蛋白由于羟化酶基因部分缺失而失去活性。我们在此报告，人类中不存在其他活性 CMP-NeuAc 羟化酶。 Southern印迹分析表明，小鼠CMP-NeuAc羟化酶的人类同源物是人类基因组中的一个基因，并且人类基因组中不存在小鼠羟化酶的其他同源物。通过荧光原位杂交，将小鼠和人类 CMP-NeuAc 羟化酶分别定位到染色体 13A3 和染色体 6p22。人羟化酶的染色体位置与小鼠羟化酶的染色体位置同线。这些结果表明，人类 CMP-NeuAc 羟化酶是小鼠羟化酶的唯一同源物，并且 CMP-NeuAc 羟化酶在人类中完全失活。 (C) 1998 年学术出版社。
We cloned cDNAs for mouse and human CMP-N-acetylneuraminic acid (CMP-NeuAc) hydroxylases and showed that the human CMP-NeuAc hydroxylase protein is inactive because of a partial deletion in the hydroxylase gene. We report here that no other active CMP-NeuAc hydroxylases are present in humans. Southern blot analysis showed that the human homologue of the mouse CMP-NeuAc hydroxylase is one gene in the human genome and no other homologues of the mouse hydroxylase exist in human genome. The mouse and the human CMP-NeuAc hydroxylases were mapped to chromosome 13A3 and chromosome 6p22, respectively, by fluorescence in situ hybridization. The chromosomal location of the human hydroxylase is syntenic to that of the mouse hydroxylase. These results demonstrate that the human CMP-NeuAc hydroxylase is the only homologue of the mouse hydroxylase, and CMP-NeuAc hydroxylase is exclusively inactive in humans. (C) 1998 Academic Press.