来自肠道寄生线虫猪蛔虫的主要胃蛋白酶抑制剂的一级结构。
Primary structure of the major pepsin inhibitor from the intestinal parasitic nematode Ascaris suum.
作者信息
Martzen M R, McMullen B A, Smith N E, Fujikawa K, Peanasky R J
机构信息
Department of Biochemistry, University of Washington, Seattle 98195.
出版信息
Biochemistry. 1990 Aug 14;29(32):7366-72. doi: 10.1021/bi00484a003.
The major pepsin inhibitor from Ascaris suum was isolated by affinity chromatography and chromatofocusing. Its amino acid sequence was determined by automated Edman degradation of peptide fragments. Peptides were produced by chemical and enzymatic cleavage of pyridylethylated protein and were purified by reverse-phase high-performance liquid chromatography. The inhibitor consists of 149 residues with the following sequence: QFLFSMSTGP10FICTVKDNQV20FVANLPWTML30EGDDIQVGKE40 FAARVEDCTN50VKHDMAPTCT60KPPPFCGPQD70MKMFNFVGCS80VLGNKLFIDQ90KYVRDLTAK D100 HAEVQTFREK110IAAFEEQQEN120QPPSSGMPHG130AVPAGGLSPP140PPPSFCTVQ149. It has a molecular weight of 16,396. All cysteines are engaged as disulfide bonds: Cys(13)-Cys(59), Cys(48)-Cys(66), and Cys(79)-Cys(146). The protein is probably composed of two domains connected by a short hydrophobic region. This is the first aspartyl protease inhibitor of animal origin that has been sequenced. The sequence has no significant homology with any other known protein.
通过亲和色谱法和色谱聚焦法从猪蛔虫中分离出主要的胃蛋白酶抑制剂。其氨基酸序列通过肽片段的自动埃德曼降解法确定。通过对吡啶基乙基化蛋白质进行化学和酶切产生肽，并通过反相高效液相色谱法进行纯化。该抑制剂由149个残基组成，序列如下：QFLFSMSTGP10FICTVKDNQV20FVANLPWTML30EGDDIQVGKE40 FAARVEDCTN50VKHDMAPTCT60KPPPFCGPQD70MKMFNFVGCS80VLGNKLFIDQ90KYVRDLTAK D100 HAEVQTFREK110IAAFEEQQEN120QPPSSGMPHG130AVPAGGLSPP140PPPSFCTVQ149。其分子量为16,396。所有半胱氨酸均形成二硫键：Cys(13)-Cys(59)、Cys(48)-Cys(66)和Cys(79)-Cys(146)。该蛋白质可能由两个结构域通过一个短的疏水区连接而成。这是首个已测序的动物源天冬氨酸蛋白酶抑制剂。该序列与任何其他已知蛋白质均无明显同源性。
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