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Kirjallisuusarvostelu

Acta martyrvm, eorvm videlicet, qvi hoc secvlo in Gallia, Germania, Anglia, Flandria, Italia, constans dederunt nomen Euangelio, idque sanguine suo obsignarunt: ab Wicleffo & Husso ad hunc vsque diem.

Translation of Le livre des martyrs, by Claude Baduel.--Cf. Brit. Mus. Cat.

Rezension von: Marita Kampshoff / Claudia Wiepcke (Hrsg.): Handbuch Geschlechterforschung und Fachdidaktik. Wiesbaden: Springer VS 2012 (512 S.) [Rezension]

Rezension von: Marita Kampshoff / Claudia Wiepcke (Hrsg.): Handbuch Geschlechterforschung und Fachdidaktik. Wiesbaden: Springer vs 2012 (512 S.; ISBN 978-3-531-18984-0)

Effect of glycosylation on the biochemical properties of beta-xylosidases from Aspergillus versicolor

Aspergillus versicolor grown on xylan or xylose produces two beta-xylosidases with differences in biochemical properties and degree of glycosylation. We investigated the alterations in the biochemical properties of these beta-xylosidases after deglycosylation with Endo-H or PNGase F. After deglycosylation, both enzymes migrated faster in PAGE or SDS-PAGE exhibiting the same R(f). Temperature optimum of xylan-induced and xylose-induced beta-xylosidases was 45A degrees C and 40A degrees C, respectively, and 35A degrees C after deglycosylation. The xylan-induced enzyme was more active at acidic pH. After deglycosylation, both enzymes had the same pH optimum of 6.0. Thermal resistance at 55A degrees C showed half-life of 15 min and 9 min for xylose- and xylan-induced enzymes, respectively. After deglycosylation, both enzymes exhibited half-lives of 7.5 min. Native enzymes exhibited different responses to ions, while deglycosylated enzymes exhibited identical responses. Limited proteolysis yielded similar polypeptide profiles for the deglycosylated enzymes, suggesting a common polypeptide core with differential glycosylation apparently responsible for their biochemical and biophysical differences.