Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
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Nakahashi Y, Taketani S, Okuda M, Inoue K, Tokunaga R
Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
Biochem Biophys Res Commun. 1990 Dec 14;173(2):748-55.
- PubMed ID
- 2260980 [ View in PubMed]
- Abstract
The cDNA encoding human ferrochelatase [EC 4.99.1.1] was isolated from a human placenta cDNA library in bacteriophage lambda gt11 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.