Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Articles Article Faculty Publications -Articles Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Purification and Biochemical Characterization of Beta-Hexosaminidase B from Freshwater CnidarianHydra vulgaris Ind-Pune Subject The topic of the resource Cnidarian; Hydra vulgaris; Lysosomal hydrolases; ?-N-Acetylhexosaminidase Description An account of the resource Beta-N-acetylhexosaminidase (Hex) is a vital lysosomal hydrolase found in all living organisms, playing a crucial role in cellular homeostasis. Dysfunctions in this enzyme are implicated in severe pathological conditions such as Tay-Sachs and Sandhoff diseases in humans. In this paper, we report the purification and biochemical characterization of hexosaminidase from the soluble extracts obtained from the polyps of Hydra vulgaris Ind Pune. The Hydra Hex was purified by two-step sequential chromatography (hydrophobic interaction and gel filtration). Our results suggested that the enzyme isoform purified from Hydra is HexB, most likely to be a homodimer with a subunit mass of 65 kD. The pH optimum was in the range of 5.0 to 6.0 and the temperature optimum in the range of 50 C to 60 C. pH stability and temperature stability were found to be 5.0 and 40C respectively. The homology modelling studies corroborated the homodimeric nature of Hydra HexB, and indicated its structural resemblance to human HexB. This study offers new insights into the biochemical characteristics of Hydra HexB, providing a foundational framework for extensive investigations on this and other lysosomal hydrolases in Hydra. In a broader context, our results significantly contribute to establishing Hydra as a potential model organism to study the lysosomal biogenesis pathway. (2024), (Association of Carbohydrate Chemists and Technologists). All Rights Reserved. Creator An entity primarily responsible for making the resource Kukkemane K.; Krishnapati L.S.; Vuruputuri R.M.; Ranganatha K.S.; Kumar N.S. Source A related resource from which the described resource is derived Trends in Carbohydrate Research, Vol-16, No. 3, pp. 60-75. Publisher An entity responsible for making the resource available Association of Carbohydrate Chemists and Technologists Date A point or period of time associated with an event in the lifecycle of the resource 2024-01-01 Identifier An unambiguous reference to the resource within a given context <a href="" target="_blank" rel="noreferrer noopener"></a> <br /><br /><a href="https://www.scopus.com/inward/record.uri?eid=2-s2.0-85209640732&amp;partnerID=40&amp;md5=2373150a91b5abd9d9c269e7d97924d7" target="_blank" rel="noreferrer noopener">https://www.scopus.com/inward/record.uri?eid=2-s2.0-85209640732&amp;partnerID=40&amp;md5=2373150a91b5abd9d9c269e7d97924d7</a> Rights Information about rights held in and over the resource Restricted Access Relation A related resource ISSN: 9750304 Format The file format, physical medium, or dimensions of the resource Online Language A language of the resource English Type The nature or genre of the resource Article Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Kukkemane K., Protein Biochemistry and Glycobiology Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, Hyderabad, 500046, India, Department of Life Sciences, School of Sciences, CHRIST University, Karnataka, Bengaluru, 560029, India; Krishnapati L.S., Protein Biochemistry and Glycobiology Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, Hyderabad, 500046, India; Vuruputuri R.M., Protein Biochemistry and Glycobiology Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, Hyderabad, 500046, India; Ranganatha K.S., Protein Biochemistry and Glycobiology Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, Hyderabad, 500046, India; Kumar N.S., Protein Biochemistry and Glycobiology Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, Hyderabad, 500046, India, University of Bremen, Bremen, Germany