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FEBS Lett. 1997 Jan 6;400(3):333-5.

Purification of ADAM 10 from bovine spleen as a TNFalpha convertase.

Author information

1
Department of Immunology, Schering-Plough Research Institute, Kenilworth, NJ 07033, USA. charles.lunn@spcorp.com

Abstract

We have purified a protease with characteristics of TNFalpha convertase from bovine spleen membranes. Peptide sequencing of the purified protein identified it as ADAM 10 (Genbank accession no. Z21961). This metalloprotease cleaves a recombinant proTNFalpha substrate to mature TNFalpha, and can cleave a synthetic peptide substrate to yield the mature TNFalpha amino terminus in vitro. The enzyme is sensitive to a hydroxamate inhibitor of MMPs, but insensitive to phosphoramidon. In addition, cloned ADAM 10 mediates proTNFalpha processing in a processing-incompetent cell line.

PMID:
9009225
DOI:
10.1016/s0014-5793(96)01410-x
[Indexed for MEDLINE]
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