Isolation and characterization of a cDNA clone for human ferritin heavy chain.
AUTOR(ES)
Boyd, D
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=391568Documentos Relacionados
- Isolation and characterization of a cDNA clone for the murine I-E beta polypeptide chain.
- cDNA clone for the heavy chain of the human B cell alloantigen DC1: strong sequence homology to the HLA-DR heavy chain.
- Nucleotide sequence of cDNA encoding rabbit ferritin L chain.
- Isolation and identification of a cDNA clone corresponding to an HLA-DR antigen beta chain.
- Nucleotide sequence of full length cDNA for a scallop striated muscle myosin heavy chain.