The primary structure of the larger subunit of soluble guanylyl cyclase from bovine lung. Homology between the two subunits of the enzyme

FEBS Lett. 1990 Jun 18;266(1-2):128-32. doi: 10.1016/0014-5793(90)81523-q.

Abstract

The primary structure of the larger subunit of the soluble guanylyl cyclase from bovine lung, which catalyzes the formation of cyclic GMP from GTP, has been determined. Two clones, isolated from two bovine libraries yielded a total of 3261 bp with a coding region of 2073 bp. The open reading frame encodes a protein of 691 amino acids and a molecular mass of 77,500. The deduced amino acid sequence reveals regions which are, to a large extent, homologous to the sequence of the smaller subunit of the enzyme as well as to the sequences of other gyanylyl and adenylyl to a large extent, homologous to the sequence of the smaller subunit of the enzyme as well as to the sequences of other gyanylyl and adenylyl cyclases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cloning, Molecular
  • DNA / genetics
  • Guanylate Cyclase / genetics*
  • Lung / enzymology
  • Macromolecular Substances
  • Molecular Sequence Data
  • Molecular Weight

Substances

  • Macromolecular Substances
  • DNA
  • Guanylate Cyclase

Associated data

  • GENBANK/X54014