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Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)

Malfroy, Bernard, Kuang, Wun-Jing, Seeburg, Peter H., Mason, Anthony J., Schofield, Peter R.·1988·FEBS Letters

Abstract

We have isolated a cDNA clone encoding human enkephalinase (neutral endopeptidase, EC 3.4.24.11) in a λgt10 library from human placenta, and present the complete 742 amino acid sequence of human enkephalinase. The human enzyme displays a high homology with rat and rabbit enkephalinase. Like the rat and rabbit enzyme, human enkephalinase contains a single N‐terminal transmembrane region and is likely to be inserted through cell membranes with the majority of protein, including its carboxy‐terminus, located extracellularly.

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Metadata

Authors
Malfroy, B., Kuang, W.-J., Seeburg, P. H., Mason, A. J., & Schofield, P. R.
Venue
FEBS Letters
Publisher
Wiley
Published
1988-02-29
Volume
229
Issue
1
Pages
206-210
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2054455131
Cited by
207
References
0
FWCI
6.56
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). https://app.cochat.ai/papers/10.1016/0014-5793(88)80828-7
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Malfroy, B., Kuang, W.-J., Seeburg, P. H., Mason, A. J., & Schofield, P. R. (1988). Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). FEBS Letters. https://doi.org/10.1016/0014-5793(88)80828-7

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