Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases

Kimm J. Hamann, Robert L. Barker, David A. Loegering, Larry R. Pease, Gerald J. Gleich

Research output: Contribution to journalArticlepeer-review

62 Scopus citations

Abstract

Several clones of human eosinophil-derived neurotoxin (EDN) cDNA have been isolated from a λgt10 cDNA library prepared from mRNA derived from noninduced HL-60 cells. The amino acid (aa) sequence deduced from the coding sequence of the EDN cDNA is identical to the aa sequence of urinary nonsecretory RNase. Comparison of the aa and/or nucleotide (nt) sequences of EDN and other proteins possessing ribonucleolytic activity, namely bovine seminal RNase, human and rat pancreatic RNases, eosinophil cationic protein (ECP), and human angiogenin, shows extensive identity at half-cystine residues and at aa of active sites. Differences in aa sequences at the active sites are often the result of single nt changes in the codons. The data presented here support the concept of a RNase gene superfamily containing secretory and nonsecretory RNases, angiogenin, EDN and ECP.

Original languageEnglish (US)
Pages (from-to)161-167
Number of pages7
JournalGene
Volume83
Issue number1
DOIs
StatePublished - Nov 15 1989

Keywords

  • Angiogenin
  • cationic protein
  • gene superfamily
  • human urinary RNase
  • nucleotide sequence
  • phage λ library

ASJC Scopus subject areas

  • Genetics

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