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

Y Watanabe, S Iwaki-Egawa, H Mizukoshi, Y Fujimoto
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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.

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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。
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