Heparinase II from Flavobacterium heparinum

Heparinase II is one of three key heparin-degrading enzymes of Flavobacterium heparinum (also known as Pedobacter heparinus1). It belongs to the polysaccharide lyases family PL21.

Heparinase II from Flavobacterium heparinum has been used:

• for digestion of heparin sulfate during exosome isolation
• for digestion of heparin sulfate in notochordal cell conditioned media (NCCM) to investigate the content of glycosaminoglycans in NCCM
• as a component of digestion buffer during cell surface glycan processing
• as a component of heparin lyase (HSase) mix to remove the heparin sulfate on the 293ͰT/ACE2 cell surface and study the effect of histones on the infectivity of pseudovirus

Heparinase II cleaves heparan sulfate, and to a lesser extent heparin (relative activity about 2:1), at the α (1-4) linkages between hexosamines and uronic acid residues (both glucuronic and iduronic), yielding mainly disaccharides. Heparinase II has the broadest substrate specificity of the three heparinases Heparinase enzymes helps in decoding the complex structures of substrates. Heparin interferes with DNA transcription in PCR and in reverse transcription of RNA. Heparinase II has been used to remove heparin for downstream analysis of genomic DNA.

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.0 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units.

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer