THE PRIMARY STRUCTURE OF A PYY-RELATED PEPTIDE FROM CHICKEN INTESTINE SUGGESTS AN ANOMALOUS SITE OF CLEAVAGE OF THE SIGNAL PEPTIDE IN PREPROPYY
THE PRIMARY STRUCTURE OF A PYY-RELATED PEPTIDE FROM CHICKEN INTESTINE SUGGESTS AN ANOMALOUS SITE OF CLEAVAGE OF THE SIGNAL PEPTIDE IN PREPROPYY
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DOI：
10.1016/0014-5793(92)81196-s
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发表时间：
1992-11-30
期刊：
影响因子：
3.5
通讯作者：
OHARTE, F
中科院分区：
文献类型：
--
作者：
CONLON, JM;OHARTE, F
尽管在脊椎动物进化过程中，胰多肽（PP）家族调节肽成员的氨基酸序列保守性较差，但肽的总长度（36个氨基酸残基）保持恒定。克隆的cDNA和/或基因组片段的核苷酸序列分析表明，PP相关序列紧随前原肽中的信号肽。从鸡肠道中分离得到一种37个氨基酸残基的酪氨酸-酪氨酸（PYY）相关肽，其一级结构为：Ala-Tyr-Pro-Pro-Lys-Pro-Glu-Ser-Pro-Gly 10-Asp-Ala-Ala-Ser-Pro-Glu-Glu-Ile-Ala-Gln 20-Tyr-Phe-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn 30-Leu-Val-Thr-Arg-Gln-Arg-Tyr. CONH 2。在肽的NH 2-末端存在额外的丙氨酸残基表明，鸡前原PYY中信号肽的切割位点不同于其它PP家族前原肽中的切割位点。
Although the amino acid sequence of members of the pancreatic polypeptide (PP)-family of regulatory peptides has been poorly conserved during vertebrate evolution, the overall length of the peptides (36 amino acid residues) has remained constant. Nucleotide sequence analysis of cloned cDNAs and/or genomic fragments has shown the PP-related sequence immediately follows the signal peptide in the prepropeptides. A peptide tyrosine-tyrosine (PYY)-related peptide with 37 residues has been isolated from the chicken intestine, and its primary structure was established as: Ala-Tyr-Pro-Pro-Lys-Pro-Glu-Ser-Pro-Gly10-Asp-Ala-Ala-Ser-Pro-Glu-Glu-Ile-Ala-Gln20-Tyr-Phe-Ser-Ala-Leu-Arg-His-Tyr-Il e-Asn30-Leu-Val-Thr-Arg-Gln-Arg-Tyr.CONH2. The presence of an additional alanine residue at the NH2-terminus of the peptide suggests that the site of cleavage of the signal peptide in chicken preproPYY is different from the site of cleavage in other PP-family prepropeptides.