Heparinase is a name for a heparin-cleaving enzyme, classified as heparin lyase in the enzyme nomenclature. It breaks specified glycosidic bonds in heparin-type polysaccharides by eliminative cleavage. The reaction identity matters when using the enzyme to perturb a complex cell-surface layer.[ref]
In a 1990 experiment, researchers perfused individual capillaries in situ with enzyme-containing solution. Heparinase treatment at least doubled tube hematocrit, the fraction of the capillary's volume occupied by red blood cells, without a significant change in red-cell velocity. Vehicle alone and heat-denatured enzyme did not produce that response.[ref]
The controls connect the response to active enzymatic treatment rather than simply perfusing fluid. The observation supports a contribution of the endothelial glycocalyx to red-cell distribution. It does not mean that hematocrit and flow velocity are the same quantity, or that one enzyme experiment completely identifies every affected surface component. The substrate specificity and preparation used remain part of the experiment's interpretation.
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