β-elimination of hyaluronate by red king crab hyaluronidase
Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial c...
Published in: | Scientific Reports |
---|---|
Main Authors: | , , , , , , , |
Format: | Text |
Language: | English |
Published: |
Nature Publishing Group UK
2021
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604925/ http://www.ncbi.nlm.nih.gov/pubmed/34799594 https://doi.org/10.1038/s41598-021-01890-3 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:8604925 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:8604925 2023-05-15T18:06:10+02:00 β-elimination of hyaluronate by red king crab hyaluronidase Sliadovskii, Dmitrii Ponomareva, Tatyana Molchanov, Maxim Pozdnyakova-Filatova, Irina Timchenko, Maria Marchenkov, Victor Gusev, Oleg Sogorin, Evgeny 2021-11-19 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604925/ http://www.ncbi.nlm.nih.gov/pubmed/34799594 https://doi.org/10.1038/s41598-021-01890-3 en eng Nature Publishing Group UK http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604925/ http://www.ncbi.nlm.nih.gov/pubmed/34799594 http://dx.doi.org/10.1038/s41598-021-01890-3 © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . CC-BY Sci Rep Article Text 2021 ftpubmed https://doi.org/10.1038/s41598-021-01890-3 2021-11-28T01:34:09Z Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show 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 that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the [Formula: see text] -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases. Text Red king crab PubMed Central (PMC) Scientific Reports 11 1 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Article |
spellingShingle |
Article Sliadovskii, Dmitrii Ponomareva, Tatyana Molchanov, Maxim Pozdnyakova-Filatova, Irina Timchenko, Maria Marchenkov, Victor Gusev, Oleg Sogorin, Evgeny β-elimination of hyaluronate by red king crab hyaluronidase |
topic_facet |
Article |
description |
Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show 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 that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the [Formula: see text] -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases. |
format |
Text |
author |
Sliadovskii, Dmitrii Ponomareva, Tatyana Molchanov, Maxim Pozdnyakova-Filatova, Irina Timchenko, Maria Marchenkov, Victor Gusev, Oleg Sogorin, Evgeny |
author_facet |
Sliadovskii, Dmitrii Ponomareva, Tatyana Molchanov, Maxim Pozdnyakova-Filatova, Irina Timchenko, Maria Marchenkov, Victor Gusev, Oleg Sogorin, Evgeny |
author_sort |
Sliadovskii, Dmitrii |
title |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_short |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_full |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_fullStr |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_full_unstemmed |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_sort |
β-elimination of hyaluronate by red king crab hyaluronidase |
publisher |
Nature Publishing Group UK |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604925/ http://www.ncbi.nlm.nih.gov/pubmed/34799594 https://doi.org/10.1038/s41598-021-01890-3 |
genre |
Red king crab |
genre_facet |
Red king crab |
op_source |
Sci Rep |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8604925/ http://www.ncbi.nlm.nih.gov/pubmed/34799594 http://dx.doi.org/10.1038/s41598-021-01890-3 |
op_rights |
© The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1038/s41598-021-01890-3 |
container_title |
Scientific Reports |
container_volume |
11 |
container_issue |
1 |
_version_ |
1766177756398223360 |