[HTML][HTML] Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer
MB Fairbanks, AM Mildner, JW Leone… - Journal of Biological …, 1999 - ASBMB
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 …
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 …
