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1: Biochem Biophys Res Commun. 1990 Dec 14;173(2):748-55.Click here to read Links

Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.

Nakahashi Y, Taketani S, Okuda M, Inoue K, Tokunaga R.

Third Department of Internal Medicine, Kansai Medical University, Osaka, Japan.

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.

PMID: 2260980 [PubMed - indexed for MEDLINE]

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