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J Biol Chem, Vol. 274, Issue 42, 29587-29590, October 15, 1999
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From the Protein Science, § Genomics Research,
Human platelet heparanase has been purified to
homogeneity and shown to consist of two, non-covalently associated
polypeptide chains of molecular masses 50 and 8 kDa. Protein sequencing
provided the basis for determination of the full-length cDNA for
this novel protein. Based upon this information and results from
protein analysis and mass spectrometry, we propose a scheme to define the structural organization of heparanase in relation to its precursor forms, proheparanase and pre-proheparanase. The 8- and 50-kDa chains
which make up the active enzyme reside, respectively, at the
NH2- and COOH-terminal regions of the inactive
precursor, proheparanase. The heparanase heterodimer is produced by
excision and loss of an internal linking segment. This paper is the
first to suggest that human heparanase is a two-chain enzyme.
Structural,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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