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. 1977 Jan;33(1):192–198. doi: 10.1128/aem.33.1.192-198.1977

Partial Purification and Some Properties of Tyrosine Phenol-Lyase from Aeromonas phenologenes ATCC 29063 1

G M Carman 1, R E Levin 1
PMCID: PMC170621  PMID: 16345185

Abstract

Tyrosine phenol-lyase was purified 32-fold from Aeromonas phenologenes ATCC 29063, the organism that produces phenol in refrigerated haddock. The purification procedure included ammonium sulfate fractionation, protamine sulfate treatment, and column chromatography with Sephadex G-200, diethyl-aminoethyl-cellulose, and hydroxyapatite. The enzyme was found to be thermally inactivated at temperatures above 40°C. The optimum pH of the enzyme was found to be pH 8.5. The Michaelis constants for l-tyrosine and pyridoxal phosphate were 2.3 × 10-4 M and 3.2 × 10-5 M, respectively. The molecular weight of tyrosine phenol-lyase was found by gel filtration and electrophoresis to be approximately 380,000.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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