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Novel Methodologies, Techniques and Technologies

Tyrosine hydroxylase (TH) is the primary enzyme involved in the biosynthesis of catecholamines in the brain. Alteration in brain TH has been observed in various neurodegenerative disorders. As a result of biochemical and physiological importance of TH, various methods have been developed for the measurement of this enzyme. However, the conventional method of TH assay is based on radiochemical determination of tritiated water produced from tritiated tyrosine substrate in presence of TH. Two buffer compositions, phosphate buffer and Trisacetate buffer have been reported earlier for the radiochemical assay of TH, without any commentary on their comparative superiority. As the assay sensitivity would have significant analytical impact while dealing with minute samples like discrete regions of mouse brain, it was rationalized to compare these two test media. The striatum from C57BL mice (eight animals per group) was homogenized with 0.5 mL of either Tris-acetate buffer (pH optima 1⁄4 7.0) or 0.1 M phosphate buffer (pH optima 1⁄4 6.8), both containing 1.0% Triton X-100. Following centrifugation in a refrigerated centrifuge, 200 uL of supernatant (sample) or respective buffer (blank) were incubated with 0.8 mCi [3H] L-tyrosine, 0.5 mM DL-6-methyl-5,6,7,8-tetrahydropyridine, 100 U catalase and 1.0 mM dithiothreitol in a total volume of 300 mL (including sample), for 20 min at 37 C. The reaction was terminated by adding 1.0 mL of stirred suspension of 7.5% (w/v) activated charcoal in 0.1 M HCl. The mixture was rapidly vortexed and centrifuged. Two hundred microliters of aliquot were transferred to the scintillation vial containing 5 mL of cocktail, for quantification of [3H] H2O in supernatant. The use of phosphate buffer resulted in 2.8-fold higher sensitivity (p < 0.01) as compared with Tris-acetate buffer.