Characterization, mapping, and expression of the human ceruloplasmin gene

F. Yang, S. L. Naylor, J. B. Lum, S. Cutshaw, J. L. McCombs, K. H. Naberhaus, J. R. McGill, G. S. Adrian, C. M. Moore, D. R. Barnett

Research output: Contribution to journalArticlepeer-review

113 Scopus citations


Ceruloplasmin (CP) is a copper-binding protein in vertebrate plasma. It is the product of an intragenic triplication and is composed of three homologous domains. Oligonucleotide probes constructed according to published amino acid sequences were used to identify cDNA clones encoding human CP. Two clones, CP-1 and CP-2, differed from each other by the presence or absence, respectively, of a deduced sequence of four amino acids. The two clones provided 81% of the sequence encoding CP. Comparison of the nucleotides of the three domains of the CP coding sequence revealed internal domain homology with identity of sequences ranging from 50.1% to 56%. The nucleotide sequence of CP-2 cDNA was compared to that of a homologous human protein, clotting factor VIII, and was found to be 48% identical overall. The CP gene was mapped to human chromosome 3 by somatic-cell-hybrid analysis and to 3q25 in situ hybridization; however, sites of hybridization to DNA on other chromosomal sites suggested additional CP-like DNA sequences in the human genome. A DNA polymorphism was detected with CP cDNA after endonuclease digestion of human DNA by Pst I. CP mRNA was detected in human liver, macrophages, and lymphocytes by in situ histohybridization.

Original languageEnglish (US)
Pages (from-to)3257-3261
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number10
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Characterization, mapping, and expression of the human ceruloplasmin gene'. Together they form a unique fingerprint.

Cite this