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arXiv · 2011.14331

Kinetic theory of Hyaluronan cleavage by Bovine Testicular Hyaluronidase in Standard and Crowded Environments

Reine Nehmé·Rouba Nasreddine·Lucija Orlic·Chrystel Lopin-Bon·Josef Hamacek·Francesco Piazza
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Abstract

${\bf Background}$ Details of the kinetic pathways governing enzymatic cleavage of hyaluronic acid (HA) by hyaluronidase are still widely uncharted. Capillary electrophoresis-based assays were used for accurate quantification of enzymatic products. A crowding agent was also employed to mimic excluded-volume constraints typical of in-vivo conditions. $ {\bf Scope}$ Introduce a comprehensive kinetic model describing the late-stage degradation of HA by hyaluronidase and identify the relevant kinetic pathways and the associated rates. ${\bf Major Conclusions}$ All relevant fragmentation and transglycosylation pathways and rates were identified. Two dimers forming a tetramer is the dominant recombination pathway. Macromolecular and self-crowding slow down the kinetics but do not alter the underlying mechanisms. ${\bf General Significance}$ Our results bring a novel and comprehensive quantitative insight into enzymatic HA degradation. Rationalizing the effect of crowding brings the intricate conditions of in-vivo settings a little closer, and also stands as a powerful tool to pinpoint relevant kinetic pathways in complex systems.

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Reine Nehmé, Rouba Nasreddine, Lucija Orlic, Chrystel Lopin-Bon, Josef Hamacek, Francesco Piazza. 2020-11-29. Kinetic theory of Hyaluronan cleavage by Bovine Testicular Hyaluronidase in Standard and Crowded Environments. https://arxiv.org/abs/2011.14331

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