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Rat atrial natriuretic factor: isolation, structure and biological activities of four major peptides.

Abstract：

:Four peptides possessing both natriuretic activity and smooth muscle relaxant activity were isolated from rat atrium and their amino acid sequences determined. The four peptides designated ANF-I, ANF-II, ANF-III and ANF-IV containing 35, 31, 30 and 25 amino acid residues, respectively, were obtained in a molar ratio of 4:60:20:16. The predominant species ANF-II, which may represent the native form of ANF, has the following sequence: (H2N)-G-P-R-S-L-R-R-S-S-C-F-G-G-R-I-D-R-I-G-A-Q-S-G-L-G-C-N-S-F-R-Y-(COO H) in which Cys-10 and Cys-26 are disulfide linked. Cleavage of the aspartyl linkage at position 16 by staphylococcal protease caused complete inactivation, indicating that the ring conformation is essential. The dose-response relationships determined for the four peptides in relaxing norepinephrine-induced contraction of rabbit thoracic aorta showed half-maximum relaxation at concentrations ranging from 1.5 X 10(-9) to 2.5 X 10(-9) M. Comparable dose-response relationships were observed in relaxation of carbacol-induced contraction of chick rectum strips as tested with ANF-II and ANF-IV.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Misono KS,Grammer RT,Fukumi H,Inagami T

doi

10.1016/0006-291x(84)90250-x

subject

Has Abstract

pub_date

1984-09-17 00:00:00

pages

444-51

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)90250-X

journal_volume

123

pub_type

杂志文章

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