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

Malfroy, B.; Kuang, W. J.; Seeburg, Peter H.; Seeburg, Peter H.; Mason, Anthony J.; Schofield, Peter R.

doi:10.1016/0014-5793(88)80828-7

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

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Seeburg, Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0014579388808287/pdf?md5=ad54a937984a97aeea59638bf4332ab8&pid=1-s2.0-0014579388808287-main.pdf
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https://doi.org/10.1016/0014-5793(88)80828-7
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引用

Malfroy, B., Kuang, W. J., Seeburg, P. H., Seeburg, P. H., Mason, A. J., & Schofield, P. R. (1988). Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). FEBS Letters, 229(1), 206-210. doi:10.1016/0014-5793(88)80828-7.

引用: https://hdl.handle.net/21.11116/0000-0000-BA25-5

要旨

We have isolated a cDNA clone encoding human enkephalinase (neutral endopeptidase, EC 3.4.24.11) in a lambda gt10 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.