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一种新型猪脑垂体前叶多肽的分离及氨基末端序列。与胰岛素原、促胰液素和劳氏肉瘤病毒转化蛋白TVFV60的同源性。

Isolation and NH2-terminal sequence of a novel porcine anterior pituitary polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus transforming protein TVFV60.

作者信息

Hsi K L, Seidah N G, De Serres G, Chrétien M

出版信息

FEBS Lett. 1982 Oct 18;147(2):261-6. doi: 10.1016/0014-5793(82)81055-7.

Abstract

An Mr 21 000 polypeptide, designated APPG, has been purified by reverse-phase, high-performance liquid chromatography (RP-HPLC), from acid extracts of porcine anterior pituitary glands. This acidic protein possesses an isoelectric point of 4.9. Amino acid analysis shows that it is not a glycoprotein and estimates it to contain about 173 amino acids. NH2-terminal sequence analysis allowed the determination of the first 50 residues unambiguously. A computer data bank search using a mutation data matrix and comparison with 269 012 protein segments indicated that this is a novel polypeptide sequence. However, this search revealed suggestive sequence homologies to a number of peptides of known sequence, including duck proinsulin (30%), Rous sarcoma virus transforming protein TVFV60 (24%) and pig secretin (26%).

摘要

一种分子量为21000的多肽,命名为APPG,已通过反相高效液相色谱(RP-HPLC)从猪垂体前叶的酸性提取物中纯化出来。这种酸性蛋白的等电点为4.9。氨基酸分析表明它不是糖蛋白,估计含有约173个氨基酸。氨基末端序列分析明确确定了前50个残基。使用突变数据矩阵进行的计算机数据库搜索以及与269012个蛋白质片段的比较表明,这是一个新的多肽序列。然而,该搜索揭示了与许多已知序列的肽存在暗示性的序列同源性,包括鸭胰岛素原(30%)、劳氏肉瘤病毒转化蛋白TVFV60(24%)和猪促胰液素(26%)。

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