一种从牛的上段肠道中高产分离出的新型多肽PHI。与胰高血糖素-促胰液素家族其他肽的关系。

A novel form of the polypeptide PHI isolated in high yield from bovine upper intestine. Relationships to other peptides of the glucagon-secretin family.

作者信息

Carlquist M, Kaiser R, Tatemoto K, Jörnvall H, Mutt V

出版信息

Eur J Biochem. 1984 Oct 15;144(2):243-7. doi: 10.1111/j.1432-1033.1984.tb08456.x.

DOI:10.1111/j.1432-1033.1984.tb08456.x

Abstract

A novel form of the polypeptide termed PHI (peptide HI with N-terminal histidine and C-terminal isoleucine amide) has been isolated from bovine upper intestine. This bovine peptide was obtained in a 40 times higher yield than the corresponding polypeptide isolated from porcine intestine. Bovine PHI is, like porcine PHI, composed of 27 amino acid residues. The complete amino acid sequence of the bovine peptide is His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Tyr-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser- Ala- Lys-Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2. This sequence differs from porcine PHI at position 10 and from human PHI at positions 10, 12 and 27. The amino acid residue exchange between porcine and bovine PHI makes the latter more similar to the vasoactive intestinal polypeptide (VIP), gastric inhibitory polypeptide (GIP), glucagon and the growth-hormone-releasing factor (GRF).

摘要

一种名为PHI（具有N端组氨酸和C端异亮氨酸酰胺的肽HI）的新型多肽已从牛的上肠中分离出来。这种牛肽的产量比从猪肠中分离出的相应多肽高出40倍。牛PHI与猪PHI一样，由27个氨基酸残基组成。牛肽的完整氨基酸序列为His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Tyr-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser-Ala-Lys-Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2。该序列在第10位与猪PHI不同，在第10、12和27位与人PHI不同。猪PHI和牛PHI之间的氨基酸残基交换使后者更类似于血管活性肠多肽（VIP）、胃抑制多肽（GIP）、胰高血糖素和生长激素释放因子（GRF）。