Rat atrial natriuretic factor: complete amino acid sequence and disulfide linkage essential for biological activity.
Rat atrial natriuretic factor: complete amino acid sequence and disulfide linkage essential for biological activity.
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DOI：
10.1016/s0006-291x(84)80279-x
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发表时间：
1984-03
影响因子：
3.1
通讯作者：
K. Misono;H. Fukumi;R. Grammer;T. Inagami
中科院分区：
文献类型：
--
作者：
K. Misono;H. Fukumi;R. Grammer;T. Inagami
测定了大鼠心房利钠肽的全氨基酸序列，该肽具有利钠和平滑肌松弛活性。该肽的结构为H 2 N-R-1 S-S-C-F-G-G-R-I-D-10 R-I-G-A-Q-S-G-L-G-C-20 N-S-F-R-Y-25 C O O H，计算分子量为2，706。发现两个半胱氨酸残基之间的二硫键形成的环结构对于利钠活性和平滑肌松弛活性都是必不可少的。纯化的肽在2× 10− 9 M浓度下引起去甲肾上腺素（5× 10− 8 M）诱导的兔胸主动脉收缩的50%舒张，在6× 10− 9 M浓度下引起完全舒张。
The complete amino acid sequence of an atrial natriuretic peptide from rat possessing both natriuretic and smooth muscle relaxant activity has been determined. The peptide has the structure H 2 N-R-1 S-S-C-F-G-G-R-I-D-10 R-I-G-A-Q-S-G-L-G-⎵ C-20 N-S-F-R-Y-25 C O O H and a calculated molecular weight of 2,706. The ring structure formed by the disulfide linkage between the two half-cystine residues was found essential for both the natriuretic activity and smooth muscle relaxant activity. The purified peptide caused 50% relaxation of norepinephrine (5× 10− 8 M) induced contraction of rabbit thoracic aorta at the concentration of 2× 10− 9 M and complete relaxation at 6× 10− 9 M.