Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
复制标题
编码人亚铁螯合酶的 cDNA 的分子克隆和序列分析。
DOI:
10.1016/s0006-291x(05)80099-3
复制
发表时间:
1990
影响因子:
3.1
通讯作者:
Rikio Tokunaga
中科院分区:
文献类型:
--
作者:
Y. Nakahashi;S. Taketani;M. Okuda;Kyoichi Inoue;Rikio Tokunaga
The cDNA encoding human ferrochelatase [EC 4.99.1.1] was isolated from a human placenta cDNA library in bacteriophage λgt11 by screening with a radiolabeled fragment of mouse ferrochelatase cDNA. The cDNA had an open reading frame of 1269 base pairs (bp) encoding a protein of 423 amino acid residues (Mr. 47,833) with alternative putative polyadenylation signals in the 3′ non-coding regions and poly (A) tails. Amino acid sequencing showed that the mature protein consists of 369 amino acid residues (Mr. 42, 158) with a putative leader sequence of 54 amino acid residues. The human enzyme showed an 88% identity to mouse enzyme and 46% to yeast enzyme. Northern blot analysis showed two mRNAs of about 2500 and 1600 bp for ferrochelatase in K562 and HepG2 cells. As full-length cDNA for human ferrochelatase is now available, molecular lesions related to erythropoietic protoporphyria can be characterized.
DOI:
10.1016/s0021-9258(18)61070-1
发表时间:
1987-07
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
P. Matsudaira
通讯作者:
P. Matsudaira
DOI:
10.1016/s0021-9258(17)44247-5
发表时间:
1983-10
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
H. Dailey;J. Fleming
通讯作者:
H. Dailey;J. Fleming