从单一动物中纯化犬血管活性肠肽。

Purification of dog VIP from a single animal.

作者信息

Wang S C, Du B H, Eng J, Chang M, Hulmes J D, Pan Y C, Yalow R S

出版信息

Life Sci. 1985 Sep 9;37(10):979-83. doi: 10.1016/0024-3205(85)90535-1.

Abstract

VIP, a potent vasodilator peptide, is reported to be identical in pig, cow, human and rat but to differ in four amino acids in chicken. This report describes the purification of dog VIP from the small intestine of a single animal. The purification method is based on tissue extraction with a sequence of organic solvents. The extracted VIP is concentrated onto cation-exchange cellulose and brought to purity by three HPLC steps. A 30% final yield of pure VIP was obtained from the original extract. Dog VIP was found to have the following sequence: His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala -Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn. Thus the amino acid sequence of dog VIP is identical with all the mammalian VIP's which have been reported. This suggests that a high degree of conservation throughout the molecule may be required for VIP bioactivity.

摘要

血管活性肠肽（VIP）是一种强效血管舒张肽，据报道，猪、牛、人及大鼠的VIP完全相同，但鸡的VIP有四个氨基酸不同。本报告描述了从一只动物的小肠中纯化犬VIP的过程。纯化方法基于用一系列有机溶剂进行组织提取。提取的VIP浓缩到阳离子交换纤维素上，并通过三步高效液相色谱法达到纯度。从原始提取物中获得了30%的纯VIP最终产率。发现犬VIP具有以下序列：His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala -Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn。因此，犬VIP的氨基酸序列与所有已报道的哺乳动物VIP相同。这表明，VIP的生物活性可能需要整个分子具有高度的保守性。