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血管紧张素II的氨基酸组成及其与血管紧张素I的生化关系。

The amino acid composition of hypertensin II and its biochemical relationship to hypertensin I.

作者信息

LENTZ K E, SKEGGS L T, WOODS K R, KAHN J R, SHUMWAY N P

出版信息

J Exp Med. 1956 Aug 1;104(2):183-91. doi: 10.1084/jem.104.2.183.

Abstract

Preparations of hypertensin II, obtained from the treatment of hypertensin I by the action of the hypertensin converting enzyme of plasma and purified by countercurrent distribution, were quantitatively analyzed for their amino acid content. Chromatography on ion exchange columns showed the presence of equimolar amounts of aspartic acid, proline, valine, isoleucine, tyrosine, phenylalanine, histidine, and arginine. Hypertensin I was found to contain one mole of leucine and one mole of histidine in addition to the amino acids of hypertensin II. These two amino acids were isolated from the conversion products of hypertensin I and identified as the peptide histidylleucine. Carboxypeptidase digestion of hypertensin I showed the carboxyl terminal sequence of amino acids to be residue-phenylalanyl-histidylleucine. Similar studies of hypertensin II demonstrated residue-phenylalanine. It was concluded that the conversion of hypertensin I by the plasma hypertensin converting enzyme involved hydrolysis of the phenylalanyl-histidine bond to form hypertensin II and histidylleucine. The further removal by carboxypeptidase of phenylalanine from hypertensin II destroyed all of the vasoconstrictor activity.

摘要

从通过血浆血管紧张素转换酶作用处理血管紧张素I并经逆流分配纯化得到的血管紧张素II制剂中,对其氨基酸含量进行了定量分析。在离子交换柱上进行色谱分析表明,存在等摩尔量的天冬氨酸、脯氨酸、缬氨酸、异亮氨酸、酪氨酸、苯丙氨酸、组氨酸和精氨酸。发现血管紧张素I除含有血管紧张素II的氨基酸外,还含有一摩尔亮氨酸和一摩尔组氨酸。从血管紧张素I的转化产物中分离出这两种氨基酸,并鉴定为肽组氨酰亮氨酸。血管紧张素I的羧肽酶消化显示氨基酸的羧基末端序列为苯丙氨酰-组氨酰亮氨酸残基。对血管紧张素II的类似研究表明为苯丙氨酸残基。得出的结论是,血浆血管紧张素转换酶对血管紧张素I的转化涉及苯丙氨酰-组氨酸键的水解,形成血管紧张素II和组氨酰亮氨酸。羧肽酶从血管紧张素II中进一步去除苯丙氨酸会破坏所有的血管收缩活性。

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Biochem J. 1945;39(5):507-15. doi: 10.1042/bj0390507.
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The purification of hypertensin II.血管紧张素II的纯化
J Exp Med. 1956 Mar 1;103(3):301-7. doi: 10.1084/jem.103.3.301.
9
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J Exp Med. 1954 Mar;99(3):275-82. doi: 10.1084/jem.99.3.275.

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