The primary structure of a plasma membrane guanylate cyclase demonstrates diversity within this new receptor family.

@article{Schulz1989ThePS,
  title={The primary structure of a plasma membrane guanylate cyclase demonstrates diversity within this new receptor family.},
  author={Stephanie Schulz and Sujay Singh and R A Bellet and Gurmit Singh and D J Tubb and Hemin Chin and David L. Garbers},
  journal={Cell},
  year={1989},
  volume={58 6},
  pages={1155-62}
}
Atrial natriuretic peptide (ANP) binds directly to a plasma membrane form of guanylate cyclase (GC-A), stimulating the production of the second messenger cyclic GMP. We show that a second guanylate cyclase/receptor (GC-B) exists, with distinctly different specificities for various natriuretic peptides. A cDNA clone encoding GC-B was isolated by low-stringency screening of a rat brain cDNA library using GC-A cDNA as a probe. The deduced amino acid sequence of GC-B is 78% identical with GC-A… CONTINUE READING

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