Primary structure of the major pepsin inhibitor from the intestinal parasitic nematode Ascaris suum.
Primary structure of the major pepsin inhibitor from the intestinal parasitic nematode Ascaris suum.
复制标题
肠道寄生线虫猪蛔虫主要胃蛋白酶抑制剂的一级结构。
DOI:
10.1021/bi00484a003
复制
发表时间:
1990
期刊:
影响因子:
2.9
通讯作者:
Peanasky,RJ
中科院分区:
文献类型:
--
作者:
Martzen,MR;McMullen,BA;Smith,NE;Fujikawa,K;Peanasky,RJ
Revised Manuscript Received May 1, 1990 abstract: 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 byreverse-phase high-performance liquid chromatography. The inhibitor consists of 149 residues with the following sequence: QFLFSMSTGP10FICTVKDNQV20FVANLPWTML30EGDDIQVGKE40-FAARVEDCTN50VKHDMAPTCT60KPPPFCGPQD70MKMFNFVGCS80VLGNKLFIDQ90KYVR-DLTAKD100HAEVQTFREK110IAAFEEQQENI20QPPSSGMPHG130AVPAGGLSPP140PPPSFCTVQ149. 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.^) ne-fourth of the world’s population and virtually all pigs are infected by the intestinal endoparasitic nematode Ascaris