Partial purification of rabbit hind brain tryptophan hydroxylase by affinity chromatography. |
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| Authors: | F Widmer B Mutus J RamaMurthy V A Sniedkus T Viswanatha |
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| Affiliation: | Department of Chemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada |
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| Abstract: | Chromatography of crude homogenates of rabbit hind brains on ε-amino caproyl-D-tryptophan methyl ester-agarose gels provide enzyme fractions with specific activity 7–10 times higher than the starting material. The activity was found to be associated with two distinct components. While nearly forty-fold increase in specific activity can be achieved by purification of the homogenate on calcium phosphate gels prior to affinity chromatography, only a single active component was noted in such prepurified extracts. |
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