Abstract
High-performance liquid chromatography was used to purify four different enzymes extracted from tobacco leaves. Phenylalanine ammonia-lyase (E.C. 4.3.1.5) and three O-methyltransferases (S-adenosyl- l-methionine: catechol O-methyltransferases, E.C. 2.1.1.6) were subjected to high-performance chomatofocusing. Parameters effecting the resolution of chromatography and the recovery of enzyme activity were investigated. The speed and high resolving power of chromatofocusing are major advantages for analytical or preparative purposes. The absorbance at 280 nm of chromatographic fractions was shown to arise mainly from small molecules and was not a measurement of protein concentration as indicated by subsequent high-performance size exclusion chromatography. Electrophoretic analysis of the active fractions on sodium dodecyl sulphate—polyacrylamide slab gels demonstrated the high degree of purification achieved by chromatofocusing.
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