Sliadovskii, D., Ponomareva, T., Molchanov, M. et al. β-elimination of hyaluronate by red king crab hyaluronidase. Sci Rep 11, 22600 (2021). https://doi.org/10.1038/s41598-021-01890-3
Sliadovskii, D., Ponomareva, T., Molchanov, M. et al. β-elimination of hyaluronate by red king crab hyaluronidase. Sci Rep 11, 22600 (2021). https://doi.org/10.1038/s41598-021-01890-3
Sliadovskii, D., Ponomareva, T., Molchanov, M. et al. β-elimination of hyaluronate by red king crab hyaluronidase. Sci Rep 11, 22600 (2021). https://doi.org/10.1038/s41598-021-01890-3
Sliadovskii, D., Ponomareva, T., Molchanov, M. et al. β-elimination of hyaluronate by red king crab hyaluronidase. Sci Rep 11, 22600 (2021). https://doi.org/10.1038/s41598-021-01890-3
Abstract
Crustacean hyaluronidases are 1 poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we have shown that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed the hyaluronidase activity of the protein roughly from40 to 50 kDa relative to the molecular marker used in electrophoresis. Analysis of the hepatopancreas transcriptome revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. It turned out that the reaction of cleavage of hyaluronate in the presence of a homogenate proceeds by the mechanism of b-elimination, which is well known for bacterial hyaluronidases. Thus, a new hyaluronidase of higher eukaryotes was found and described, which is not integrated into the modern classification of hyaluronidases.
Biology and Life Sciences, Biochemistry and Molecular Biology
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