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

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...

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Veröffentlicht in:	FEBS letters 1988-10, Vol.239 (1), p.29-34
Hauptverfasser:	Koesling, Doris, Herz, Joachim, Gausepohl, Heinrich, Niroomand, Feraydoon, Hinsch, Klaus-Dieter, Mülsch, Alexander, Böhme, Eycke, Schultz, Günter, Frank, Rainer
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Cattle cDNA sequence Cloning, Molecular DNA - genetics Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Guanylate cyclase Guanylate Cyclase - genetics Lung - enzymology Lyases Macromolecular Substances Molecular Sequence Data Molecular Weight Peptide antibody
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(88)80539-8