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从人血浆蛋白的科恩III-O组分中纯化具有血管收缩和血管舒张活性的肽。

Purification of a peptide with venoconstrictor and vasodepressor activity, from Cohn fraction III-O of human plasma protein.

作者信息

Horowitz J D, Mashford M L

出版信息

Vox Sang. 1980;38(5):259-65. doi: 10.1111/j.1423-0410.1980.tb02365.x.

DOI:10.1111/j.1423-0410.1980.tb02365.x
PMID:7415072
Abstract

Cohn fraction III-O of human plasma proteins has previously been shown to contain a peptide which produces vasodilator responses in intact vascular beds. This peptide has bradykinin-like pharmacological actions but it can be distinguished from bradykinin. A process of serial fractionation of Cohn fraction III-O on Sephadex CM-25 and G-25 gels, followed by ion exchange chromatography with gradient elution on a Bio-Rex 70 column and subsequent desalting has permitted purification of this peptide. Amino acid analysis suggested a peptide with 14 amino acyl-residues and a calculated molecular weight of 1,780. The purified material retained the vasodilator properties of impure sources of the peptide, but was highly unstable. There was no interaction with anti-bradykinin antibodies.

摘要

人血浆蛋白的科恩III - O级分先前已被证明含有一种在完整血管床中产生血管舒张反应的肽。这种肽具有类似缓激肽的药理作用,但可与缓激肽区分开来。通过在葡聚糖凝胶CM - 25和G - 25上对科恩III - O级分进行连续分级分离,随后在Bio - Rex 70柱上进行梯度洗脱离子交换色谱以及后续脱盐,已实现该肽的纯化。氨基酸分析表明该肽含有14个氨基酸残基,计算分子量为1780。纯化后的物质保留了该肽不纯来源的血管舒张特性,但高度不稳定。它与抗缓激肽抗体没有相互作用。

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