AI Article Synopsis
- A new affinity gel using L-Tyrosine was developed for purifying bovine testicular hyaluronidase (BTH) through a method involving cyanogen bromide-activated Sepharose-4B with m-Anisidine as a ligand.
- The purification process achieved a yield of 16.95% and a high purity level of 881.78%.
- Kinetic analysis showed that the Michaelis constant (K(M)) for BTH was 2.23 mM and the maximum reaction rate (V(Max)) was 19.85 U/mL, with gibberellic acid identified as the strongest inhibitor of the enzyme among tested chemicals.
Article Abstract
In 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 2.23 mM 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, β-naphthoxyacetic acid and gibberellic acid. Gibberellic acid showed the best inhibition effect on BTH.
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| http://dx.doi.org/10.3109/14756366.2014.949253 | DOI Listing |
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