Literature summary for 3.2.1.166 extracted from

Fairbanks, M.B.; Mildner, A.M.; Leone, J.W.; Cavey, G.S.; Mathews, W.R.; Drong, R.F.; Slightom, J.L.; Bienkowski, M.J.; Smith, C.W.; Bannow, C.A.; Heinrikson, R.L.
Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer (1999), J. Biol. Chem., 274, 29587-29590.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
50000	-	1 * 50000 + 1 * 80000, SDS-PAGE	Homo sapiens
80000	-	1 * 50000 + 1 * 80000, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y251	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the 8000 Da and 50000 Da chains which make up the active enzyme reside, respectively, at the NH2-terminal and COOH-terminal regions of the inactive precursor, proheparanase. The heparanase heterodimer is produced by excision and loss of an internal linking segment	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood platelet	-	Homo sapiens	-

Subunits

Subunits	Comment	Organism
dimer	1 * 50000 + 1 * 80000, SDS-PAGE	Homo sapiens

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Release 2023.1 (January 2023)