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. 1984 Aug;81(15):4751–4755. doi: 10.1073/pnas.81.15.4751

Isolation and characterization of a cDNA clone for human ferritin heavy chain.

D Boyd, S K Jain, J Crampton, K J Barrett, J Drysdale
PMCID: PMC391568  PMID: 6589621

Abstract

Ferritin, the main iron-storage protein, is composed of two partially homologous subunits, heavy (H) and light (L), with MrS of 21,000 and 19,000, respectively. We have isolated a cDNA clone for human ferritin H chains by screening a human lymphocyte cDNA library with synthetic oligodeoxyribonucleotides. The oligonucleotide sequences were derived from two 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. These results indicate that the cloned DNA 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, we conclude that 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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