Molecular characterization of human and bovine endothelin converting enzyme 
(ECE-1)

Schmidt, Martin; Kröger, Burkhard; Jacob, Elard; Seulberger, Harald; Subkowski, Thomas; Otter, Rainer; Meyer, Thomas; Schmalzing, Günther; Hillen, Heinz

doi:10.1016/0014-5793(94)01277-6

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Molecular characterization of human and bovine endothelin converting enzyme (ECE-1)

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Schmalzing, Günther
Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schmidt, M., Kröger, B., Jacob, E., Seulberger, H., Subkowski, T., Otter, R., et al. (1994). Molecular characterization of human and bovine endothelin converting enzyme (ECE-1). FEBS Letters, 356(2-3), 238-243. doi:10.1016/0014-5793(94)01277-6.

Cite as: https://hdl.handle.net/21.11116/0000-0008-32A4-6

Abstract

A membrane-bound protease activity that specifically converts Big endothelin-1 has been purified from bovine endothelial cells (FBHE). The enzyme was cleaved with trypsin and the peptide sequencing analysis confirmed it to be a zinc chelating metalloprotease containing the typical HEXXH (HELTH) motif. RT-PCR and cDNA screens were employed to isolate the complete cDNAs of the bovine and human enzymes. This human metalloprotease was expressed heterologously in cell culture and oocytes. The catalytic activity of the recombinant enzyme is the same as that determined for the natural enzyme. The data suggest that the characterized enzyme represents the functional human endothelin converting enzyme ECE-1.