Isolation and characterization of a cDNA clone for human ferritin heavy chain.
- 1 August 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (15) , 4751-4755
- https://doi.org/10.1073/pnas.81.15.4751
Abstract
Ferritin, the main Fe-storage protein, is composed of 2 partially homologous subunits, heavy (H) and light (L), with MW of 21,000 and 19,000, respectively. A cDNA [complementary DNA] clone for human ferritin H chains was isolated by screening a human lymphocyte cDNA library with synthetic oligodeoxyribonucleotides. The oligonucleotide sequences were derived from 2 pentapeptides found in human spleen ferritin. The selected clone hybridized to both probes and selected H-chain mRNA, but not L-chain mRNA, when hybridized to HeLa cell mRNA. The cloned DNA probably codes for a H chain of human ferritin. Since the amino acid sequence derived from the cloned DNA was almost identical to the partial amino acid sequence of a minor component found in human spleen ferritin, the minor sequence found in human spleen ferritin must be a H subunit. Genomic analysis gives a complex pattern that suggests that ferritin H chains are encoded by a multigene family or have an unusually large number of exons.Keywords
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