Amyloidosis pp 61-68 | Cite as

Human Serum Amyloid Genes — Molecular Characterization

  • George H. SackJr.
  • John J. Lease


Three clones containing human genes for serum amyloid A protein (SAA) have been isolated and characterized. Each of two clones, GSAA 1 and 2 (of 12.8 and 15.9 kilobases, respectively), contains two exons, accouting for amino acids 12–58 and 58–103 of mature SAA; the extreme 5′ termini and 5′ untranslated regions have not yet been defined but are anticipated to be close based on studies of murine SAA genes. Initial amino acid sequence comparisons show 78/89 identical residues. At 4 of the 11 discrepant residues, the amino acid specified by the codon is the same as the corresponding residue in murine SAA. Identification of regions containing coding regions has permitted use of selected subclones for blot hybridization studies of larger human SAA chromosomal gene organization. The third clone, GSAA 3 also contains SAA coding information by DNA sequence analysis but has a different organization which has not yet been fully described.

We have reported the isolation of clones of human DNA hybridizing with pRS48 — a plasmid containing a complementary DNA (cDNA) clone for murine serum amyloid A (SAA; 1, 2). We now present more detailed data confirming the identity and defining some of the organizational features of these clones.


Reiteration Frequency Murine Serum Amyloid 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • George H. SackJr.
    • 1
    • 2
    • 3
    • 4
    • 5
  • John J. Lease
    • 1
    • 2
    • 3
    • 4
    • 5
  1. 1.Department of MedicineThe John Hopkins University School of MedicineUSA
  2. 2.Department of Biological ChemistryThe John Hopkins University School of MedicineUSA
  3. 3.Department of OrthopedicsThe John Hopkins University School of MedicineUSA
  4. 4.Department of PediatricsThe John Hopkins University School of MedicineUSA
  5. 5.The John F. Kennedy InstituteBaltimoreUSA

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