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Protein Expr Purif. 2001 Feb;21(1):65-70.

Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin.

Author information

  • 1Department of Biochemistry I, Faculty of Chemistry, University of Bielefeld, 33615 Bielefeld, Germany.

Abstract

ADAM 9 is a member of the cellular metalloprotease/disintegrin/cysteine-rich (MDC) gene family, related to soluble snake venom metalloproteases (SVMP). ADAMs may play important roles in cell-cell fusion, cell-matrix interaction, and other cellular functions. To investigate catalytic activity of human ADAM 9 we have cloned and expressed the metalloprotease domain of human ADAM 9 in Pichia pastoris. The recombinant protein was purified in a three-step purification procedure and activity was detected against gelatin, beta-casein, and fibronectin. In addition we identified five normal and cancer cell lines expressing mRNA of human ADAM 9.

Copyright 2001 Academic Press.

PMID:
11162388
[PubMed - indexed for MEDLINE]
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