人母血清丙氨酸氨基肽酶的膜结合氨基肽酶N的鉴定。

Y Watanabe, S Iwaki-Egawa, H Mizukoshi, Y Fujimoto
{"title":"人母血清丙氨酸氨基肽酶的膜结合氨基肽酶N的鉴定。","authors":"Y Watanabe,&nbsp;S Iwaki-Egawa,&nbsp;H Mizukoshi,&nbsp;Y Fujimoto","doi":"10.1515/bchm3.1995.376.7.397","DOIUrl":null,"url":null,"abstract":"<p><p>In addition to cystine aminopeptidase (oxytocinase) alanine aminopeptidase is present at high levels in the serum of pregnant women. In this study we compared the enzyme with membrane-bound aminopeptidase N purified from human placenta. Comparison of catalytic and immunological properties and N-terminal sequence analyses revealed that the enzymes were differentially processed derivatives of the same protein, and that the N-terminal 68 residues of aminopeptidase N were deleted in the alanine aminopeptidase. The deleted sequence contains a small cytoplasmic region, a hydrophobic transmembrane domain and a junctional domain. These results suggest that the enzyme may be released into the maternal circulation as a result of lacking these three domains.</p>","PeriodicalId":8963,"journal":{"name":"Biological chemistry Hoppe-Seyler","volume":"376 7","pages":"397-400"},"PeriodicalIF":0.0000,"publicationDate":"1995-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm3.1995.376.7.397","citationCount":"18","resultStr":"{\"title\":\"Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N.\",\"authors\":\"Y Watanabe,&nbsp;S Iwaki-Egawa,&nbsp;H Mizukoshi,&nbsp;Y Fujimoto\",\"doi\":\"10.1515/bchm3.1995.376.7.397\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>In addition to cystine aminopeptidase (oxytocinase) alanine aminopeptidase is present at high levels in the serum of pregnant women. In this study we compared the enzyme with membrane-bound aminopeptidase N purified from human placenta. Comparison of catalytic and immunological properties and N-terminal sequence analyses revealed that the enzymes were differentially processed derivatives of the same protein, and that the N-terminal 68 residues of aminopeptidase N were deleted in the alanine aminopeptidase. The deleted sequence contains a small cytoplasmic region, a hydrophobic transmembrane domain and a junctional domain. These results suggest that the enzyme may be released into the maternal circulation as a result of lacking these three domains.</p>\",\"PeriodicalId\":8963,\"journal\":{\"name\":\"Biological chemistry Hoppe-Seyler\",\"volume\":\"376 7\",\"pages\":\"397-400\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/bchm3.1995.376.7.397\",\"citationCount\":\"18\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biological chemistry Hoppe-Seyler\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/bchm3.1995.376.7.397\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biological chemistry Hoppe-Seyler","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/bchm3.1995.376.7.397","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 18

摘要

除了胱氨酸氨基肽酶(催产素酶)外,丙氨酸氨基肽酶在孕妇血清中含量也很高。本研究将该酶与从人胎盘中纯化的膜结合氨基肽酶N进行了比较。催化和免疫特性的比较以及N端序列分析表明,这两种酶是同一蛋白的差异加工衍生物,并且在丙氨酸氨基肽酶中N端68个残基被删除。删除的序列包含一个小的细胞质区,一个疏水跨膜结构域和一个连接结构域。这些结果表明,由于缺乏这三个结构域,酶可能被释放到母体循环中。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N.

In addition to cystine aminopeptidase (oxytocinase) alanine aminopeptidase is present at high levels in the serum of pregnant women. In this study we compared the enzyme with membrane-bound aminopeptidase N purified from human placenta. Comparison of catalytic and immunological properties and N-terminal sequence analyses revealed that the enzymes were differentially processed derivatives of the same protein, and that the N-terminal 68 residues of aminopeptidase N were deleted in the alanine aminopeptidase. The deleted sequence contains a small cytoplasmic region, a hydrophobic transmembrane domain and a junctional domain. These results suggest that the enzyme may be released into the maternal circulation as a result of lacking these three domains.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信