Purification of an acidic coniferin-hydrolysing beta-glucosidase from developing xylem of Pinus banksiana.
Two cytosolic, acidic (pI 3.8) glycoproteins (M(r) 110,000 and 90,000) from lignifying xylem of Pinus banksiana were electrophoretically isolated and confirmed by combined gas chromatography-mass spectrometry to be capable of hydrolysing E-coniferin to trans-coniferyl alcohol. These isoenzymes yielded identical N-terminal sequences having negligible homology with documented glucosidases, suggesting that they constitute a novel form of beta-glucosidase.
Leinhos
V
V
FSU Jena, Institut für Ernährung und Umwelt, Germany.
Udagama-Randeniya
P V
PV
Savidge
R A
RA
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D002934:Cinnamates / Q000378:metabolism*; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D014197:Trees / Q000201:enzymology* / Q000254:growth & development; D001617:beta-Glucosidase / Q000302:isolation & purification* / Q000378:metabolism
D002934:Cinnamates; D001617:beta-Glucosidase; C016316:coniferin