Journal article

BETA-GALACTOSIDASES OF LILIUM POLLEN

MB SINGH, RB KNOX

PHYTOCHEMISTRY | PERGAMON-ELSEVIER SCIENCE LTD | Published : 1985

Abstract

Lily (Lilium auratum) pollen contains very high levels of β-galactosidase. There are three forms: β-galactosidase I and II differ in Mr, while β-galactosidase III is firmly bound in the pollen wall. The two cytoplasmic forms were separated and partially purified using a combination of chromatography on DEAE-cellulose, Sephadex G-200 and Sepharose 6B. Forms I and II appear to be glycoprotein in nature as shown by binding to Con A-Sepharose. The three enzymes were optimally active near pH 4, and all were inhibited by galactose and galactonolactone. The wall-bound enzyme, β-galactosidase III effectively hydrolysed nitrophenyl β-galactosidase but not lactose, and could not be released from the w..

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University of Melbourne Researchers