Characterization and primary sequence of a human hepatic microsomal estriol UDPglucuronosyltransferase.

Characterization and primary sequence of a human hepatic microsomal estriol UDPglucuronosyltransferase.
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人肝微粒体雌三醇 UDP 葡萄糖醛酸基转移酶的表征和一级序列。

DOI:
10.1016/0003-9861(90)90428-2
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发表时间:
1990
影响因子:
3.9
通讯作者:
Burchell,B
Burchell,B
中科院分区:
生物学3区
文献类型:
--
作者:
Coffman,BL;Tephly,TR;Irshaid,YM;Green,MD;Smith,C;Jackson,MR;Wooster,R;Burchell,B

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人肝微粒体UDPglucuronosyltransferase (UDPGT)显示出与雌三醇(pI7.4 UDPGT)的反应性,已经纯化到均匀性并进一步表征。对吗啡、4-羟基联苯、胆红素或三烯胺无活性。雌三醇UDPGT对大鼠肝微粒体3α-和17β-羟基类固醇UDPGT抗体有免疫反应性,但对大鼠肝微粒体-硝基酚UDPGT抗体无免疫反应性。对纯化蛋白的nh2末端序列进行了测定,发现其与λgt11 (HLUG4)中从人肝脏文库中导出的cDNA氨基酸序列一致。序列分析表明,HLUG4全长2094 bp,编码523个氨基酸的蛋白,其中有一个16个氨基酸的先导序列,后面是一个525 bp的未翻译3 '区。在预测序列中确定了三个潜在的n -糖基化位点。雌三醇UDPGT的氨基酸序列与另一个人肝脏cDNA (HLUG25)的氨基酸序列具有82%的同源性,HLUG25已被表达为能够羟基脱氧胆酸6α-羟基葡萄糖醛酸化的UDPGT,这强烈表明这些蛋白是同一基因亚家族的成员。
A human liver microsomal UDPglucuronosyltransferase (UDPGT) that demonstrates reactivity with estriol (pI7.4 UDPGT) has been purified to homogeneity and characterized further. No activity toward morphine, 4-hydroxybiphenyl, bilirubin, or tripelennamine was observed. The estriol UDPGT shows immunoreactivity with antibodies raised against rat hepatic microsomal 3α- and 17β-hydroxysteroid UDPGTs but not with antibodies raised against rat hepatic microsomalp-nitrophenol UDPGT. The NH2-terminal sequence of the purified protein was determined and found to correspond to an identical sequence in the deduced amino acid sequence of a cDNA obtained from a human liver library in λgt11 (HLUG4). Sequence analysis revealed that HLUG4 is 2094 bp in length and encodes a protein of 523 amino acids which has a 16 amino acid leader sequence, followed by an untranslated 3′ region of 525 bp. Three potential N-glycosylation sites were identified in the predicted sequence. The deduced amino acid sequence of estriol UDPGT showed 82% identity with the deduced amino acid sequence of another human hepatic cDNA (HLUG25), which has been expressed as a UDPGT capable of 6α-hydroxyglucuronidation of hyodeoxycholic acid, strongly suggesting that these proteins are members of the same gene subfamily.
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