PMID: 9530881Apr 8, 1998Paper

Purification and characterization of lanatoside 15'-O-acetylesterase from Digitalis lanata Ehrh

Planta
R KandziaM Luckner

Abstract

Lanatoside 15'-O-acetylesterase (LAE) from in-vitro-cultivated cells of Digitalis lanata Ehrh. was isolated and partially sequenced. The enzyme was extracted with citrate buffer from acetone dry powder. It was purified in a two-step chromatographical procedure including Phenyl Sepharose hydrophobic interaction chromatography followed by CM Sepharose cation-exchange chromatography to more than 330 mumol.s-1.(g protein)-1. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified protein showed a major band at 39 kDa. The protein was identified by correlation of band intensity on SDS-PAGE and enzyme activity of CM Sepharose column fractions. Size-exclusion chromatography on Sephacryl 200 revealed a single activity peak with an apparent molecular mass of about 85 kDa. Electrophoresis under nondenaturating conditions of purified LAE showed only one band with esterase activity. The intensity of this band was correlated with that of the 39-kDa band after SDS-PAGE. About 30% of the protein, including the N-terminus and several fragments obtained by Lys-C protease digestion, was sequenced. A fragment obtained by Lys-C digestion showed partial homology to other hydrolases and apoplasmic proteins. It included t...Continue Reading

Citations

Aug 22, 2000·Biopolymers·P RydenS G Ring
Apr 6, 2004·Plant Physiology and Biochemistry : PPB·David Pringle, Rebecca Dickstein
May 10, 2003·Phytochemistry·Vinod Shanker DubeyRajesh Luthra
Mar 7, 2008·Molecular Plant-microbe Interactions : MPMI·Laurent CoqueRebecca Dickstein
Oct 11, 2003·Journal of Biochemistry and Molecular Biology·Kyung-Ah Lee, Tae-Ju Cho
Oct 5, 2016·Bioscience, Biotechnology, and Biochemistry·Taiji Nomura

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