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首页> 外文期刊>FEBS Letters >Isolation and characterization of proSS1–32, a peptide derived from the N‐terminal region of porcine preprosomatostatin
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Isolation and characterization of proSS1–32, a peptide derived from the N‐terminal region of porcine preprosomatostatin

机译:proSS1-32的分离和鉴定,proSS1-32是源自猪前前列腺抑素N端区域的肽

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>A peptide derived from the N-terminal region of porcine prosomatostatin, proSS1–32, has been purified to homogeneity from extracts of porcine upper intestine. Amino acid analysis revealed that the peptide consists of 32 residues. The complete primary structure was determined as: A P S D P R L R Q F L Q K S L A A A A G K Q E L A K Y F L A E L This sequence obviously comprises residues 1–32 of porcine prosomatostatin since it is identical to the corresponding sequence in human preprosomatostatin. The postulated cleavage site in porcine prosomatostatin is a Leu-Leu bond between residues 32 and 33, thus confirming previous studies of the processing of the somatostatin precursor in the rat and transgenic mouse.
机译:>从猪前列腺抑素N端区域衍生的肽proSS 1-32 已从猪上肠提取物中纯化至同质。氨基酸分析表明该肽由32个残基组成。完整的一级结构确定为:A P A D A R A Q A L A L E L该序列显然包含猪前列腺抑素的1-33位残基,因为它与人前列腺素原中的相应序列相同。猪前列腺抑素中假定的切割位点是残基32和33之间的Leu-Leu键,因此证实了以前在大鼠和转基因小鼠中处理生长抑素前体的研究。

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