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H2519 Sigma-Aldrich

Heparinase I from Flavobacterium heparinum

Lyophilized powder stabilized with approx. 25% bovine serum albumin, ≥200 units/mg protein (enzyme + BSA)

Synonym: Heparin lyase I, Heparinase

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Description

Application

Heparinase I from Flavobacterium heparinum has been used:
• in the digestion of plasma samples
• to study the effect of medium, washing and sonication on the infectivity of Chlamydia pneumonia
• in enzymatic removal of heparan sulfate from the surface of human rhabdomyosarcoma cells

Biochem/physiol Actions

Heparinase I from Flavobacterium heparinum acts by cleaving the α-glycoside linkage at AT III binding site in heparin. This results in small oligosaccharide fragments and heparinase I neutralizes the protein′s action of anticoagulation. Therefore it might replace the use of protamine in reversing heparin induced anticoagulation after coronary artery bypass surgery. Heparinase I possesses a half-life of 15-18 minutes.

Unit Definition

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units.

Other Notes

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

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable
Protocols & Articles

Articles

Glycosaminoglycan Sulfation and Signaling

Glycosaminoglycans are large linear polysaccharides constructed of repeating disaccharide units. The disaccharide units that are the basis of all glycosaminoglycans (except keratan) are a combination...
Vicki Caligur
BioFiles 2008, 3.10, 4.
Keywords: Adhesion, Aminations, Angiogenesis, Anticoagulants, Apoptosis, Atomic absorption spectroscopy, Cancer, Cell biology, Cell proliferation, Cell signaling, Cellular processes, Central Nervous System, Chromatography, Coagulation, Degradations, Enzyme-linked immunosorbent assay, Epimerizations, Gene expression, Genetic, Genomics, Growth factors, Help, High performance liquid chromatography, Inflammation, Ion-exchange chromatography, Ligands, Mass spectrometry, Methods, Microarray Analysis, Morphogenesis, Nuclear magnetic resonance spectroscopy, Phosphorylations, Polymerase chain reaction, Polymerization reactions, Proteomics, Reductive aminations, Sequences, Spectroscopy, Sulfations, Transcription, Type, transformation

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Peer-Reviewed Papers
15

References

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