Tatemoto K, Mutt V
Proc Natl Acad Sci U S A. 1981 Nov;78(11):6603-7. doi: 10.1073/pnas.78.11.6603.
A new peptide, designated PHI (PHI-27), has been discovered and isolated from porcine upper intestinal tissue by using a chemical method for finding peptide hormones and other active peptides. The method is based on chemical detection of peptides having the cOOH-terminal alpha-amide structure, which is an unusual chemical feature of some peptide hormones and active peptides. Porcine PHI was found in the intestinal extract by the presence of its COOH-terminal isoleucine amide structure. It consists of 27 amino acid residues and has the following amino acid sequence: His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Phe-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser-Ala-Lys -Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2. The remarkable sequence homology of PHI to the vasoactive intestinal peptide, secretin, glucagon, and gastric inhibitory polypeptide indicates that this peptide is a member of the glucagon-secretin family. Several biological activities of PHI, similar to those of vasoactive intestinal peptide and secretin, have been reported.
一种新的肽，命名为PHI（PHI - 27），已通过一种用于发现肽类激素和其他活性肽的化学方法从猪的上肠道组织中发现并分离出来。该方法基于对具有COOH末端α - 酰胺结构的肽的化学检测，这是一些肽类激素和活性肽的一种不寻常化学特征。通过其COOH末端异亮氨酸酰胺结构的存在，在肠道提取物中发现了猪PHI。它由27个氨基酸残基组成，具有以下氨基酸序列：His - Ala - Asp - Gly - Val - Phe - Thr - Ser - Asp - Phe - Ser - Arg - Leu - Leu - Gly - Gln - Leu - Ser - Ala - Lys - Lys - Tyr - Leu - Glu - Ser - Leu - Ile - NH2。PHI与血管活性肠肽、促胰液素、胰高血糖素和胃抑制多肽具有显著的序列同源性，表明该肽是胰高血糖素 - 促胰液素家族的成员。已报道PHI的几种生物学活性，类似于血管活性肠肽和促胰液素的活性。
