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Updated: Feb 21, 2026

Rapid Point-of-Care Assay of Enoxaparin Anticoagulant Efficacy in Whole Blood
Published on: October 12, 2012
Immobilization alters heparin cleaving properties of heparinase I
Indu Bhushan1,2,3, Alhumaidi Alabbas1,4,5, Balagurunathan Kuberan6
1Institute for Structural Biology, Drug Discovery and Development.
Abstract:
We report here a novel observation that immobilization of heparinase I on CNBr-activated Sepharose results in heparin degradation properties that are different from heparinase I in the free solution form. Studies over a range of pHs (5-8) and temperatures (5-50°C) as well as under batch and flow conditions show that immobilized heparinase 1 displays altered pH and temperature optima, and a higher propensity for generation of longer chains (hexa- and octa-) with variable sulfation as compared to that in the free form, which is known to yield disaccharides. The immobilized enzyme retained good eliminase activity over at least five cycles of reuse. In combination, results suggest that heparinase I immobilization may offer a more productive route to longer, variably sulfated sequences.
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