Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N.

Y Watanabe, S Iwaki-Egawa, H Mizukoshi, Y Fujimoto
{"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}
引用次数: 18

Abstract

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.

人母血清丙氨酸氨基肽酶的膜结合氨基肽酶N的鉴定。
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。
求助全文
约1分钟内获得全文 求助全文
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