The primary structure of the 70 kDa subunit of bovine soluble guanylate cyclase

Doris Koesling, Joachim Herz, Heinrich Gausepohl, Feraydoon Niroomand, Klaus Dieter Hinsch, Alexander Mülsch, Eycke Böhme, Günter Schultz, Rainer Frank

Research output: Contribution to journalArticlepeer-review

114 Scopus citations

Abstract

The primary structure of the 70 kDa subunit of soluble bovine guanylate cyclase, which catalyzes the formation of cyclic GMP from GTP, has been determined. The alignment of six different clones out of two bovine libraries yielded a total of 3.1 kb with a coding region of 1857 bases. The open reading frame encodes a protein of 619 amino acids and a molecular mass of 70.5 kDa. Antibodies raised against a synthetic peptide, which corresponded to the C-terminus of the deduced sequence precipitated guanylate cyclase activity from guanylate cyclase-enriched preparations.

Original languageEnglish (US)
Pages (from-to)29-34
Number of pages6
JournalFEBS Letters
Volume239
Issue number1
DOIs
StatePublished - Oct 24 1988

Keywords

  • Guanylate cyclase
  • Peptide antibody
  • cDNA sequence

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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