Amino acid sequence of homologous rat atrial peptides: natriuretic activity of native and synthetic forms.

AUTOR(ES)

Seidah, N G

RESUMO

A substance called atrial natriuretic factor (ANF), localized in secretory granules of atrial cardiocytes, was isolated as four homologous natriuretic peptides from homogenates of rat atria. The complete sequence of the longest form showed that it is composed of 33 amino acids. The three other shorter forms (2-33, 3-33, and 8-33) represent amino-terminally truncated versions of the 33 amino acid parent molecule as shown by analysis of sequence, amino acid composition, or both. The proposed primary structure agrees entirely with the amino acid composition and reveals no significant sequence homology with any known protein or segment of protein. The short form ANF-(8-33) was synthesized by a multi-fragment condensation approach and the synthetic product was shown to exhibit specific activity comparable to that of the natural ANF-(3-33).

Documentos Relacionados

• Natriuretic Peptides: New Players in Energy Homeostasis
• Natriuretic peptides: are these new links in the hepatorenal connections?
• Colony-stimulating activity induced by synthetic muramyl peptides: variation with chemical structure and association with anti-infectious activity.
• Evidence for a new role of natriuretic peptides: control of intraocular pressure.
• Protective immunogenicity of two synthetic peptides selected from the amino acid sequence of Bordetella pertussis toxin subunit S1.