A new affinity method for purification of bovine testicular hyaluronidase enzyme and an investigation of the effects of some compounds on this enzyme

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dc.authoridKAYA, Mustafa Oguzhan/0000-0002-8592-1567
dc.contributor.authorKaya, Mustafa Oguzhan
dc.contributor.authorArslan, Oktay
dc.contributor.authorGuler, Ozen Ozensoy
dc.date.accessioned2024-12-24T19:30:59Z
dc.date.available2024-12-24T19:30:59Z
dc.date.issued2015
dc.departmentSiirt Üniversitesi
dc.description.abstractIn this study, a new affinity gel for the purification of bovine testicular hyaluronidase (BTH) was synthesized. L-Tyrosine was added as the extension arm to the Sepharose-4B activated with cyanogen bromide. m-Anisidine is a specific inhibitor of BTH enzyme. m-Anisidine was clamped to the newly formed Sepharose-4B-L-tyrosine as a ligand. As a result, an affinity gel having the chemical structure of Sepharose-4B-L-tyrosine-m-anisidine was obtained. BTH purified by ammonium sulfate precipitation and affinity chromatography was obtained with a 16.95% yield and 881.78 degree of purity. The kinetic constants K-M and V-Max for BTH were determined by using hyaluronic acid as a substrate. K-M and V-Max values obtained from the Lineweaver-Burk graph were found to be 2.23mM and 19.85 U/mL, respectively. In vitro effects of some chemicals were determined on purified BTH enzyme. Some chemically active ingredients were 1,1-dimethyl piperidinium chloride, beta-naphthoxyacetic acid and gibberellic acid. Gibberellic acid showed the best inhibition effect on BTH.
dc.description.sponsorshipBalikesir University [2012/38]
dc.description.sponsorshipThis work was supported by a Balikesir University Research Project (2012/38) and carried out at the Balikesir University Research Center of Applied Sciences (BURCAS).
dc.identifier.doi10.3109/14756366.2014.949253
dc.identifier.endpage527
dc.identifier.issn1475-6366
dc.identifier.issn1475-6374
dc.identifier.issue4
dc.identifier.pmid25373501
dc.identifier.scopus2-s2.0-84937204862
dc.identifier.scopusqualityQ1
dc.identifier.startpage524
dc.identifier.urihttps://doi.org/10.3109/14756366.2014.949253
dc.identifier.urihttps://hdl.handle.net/20.500.12604/7756
dc.identifier.volume30
dc.identifier.wosWOS:000359816600002
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Ltd
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_20241222
dc.subjectAffinity chromatography
dc.subjectbovine testicular hyaluronidase
dc.subjectinhibition
dc.titleA new affinity method for purification of bovine testicular hyaluronidase enzyme and an investigation of the effects of some compounds on this enzyme
dc.typeArticle

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