title: Properties of alpha-mannosidase partially purified from the apple snail, Pomacea canaliculata.
abstract: Pomacea canaliculata alpha-mannosidase (260 kDa), composed of at least two isoforms with different pI, was partially purified. The activity was maximum at pH 4 and unaltered after incubation at 60 degrees C for 60 min. ZnCl2, CaCl2, NaCl, and SH-reagents increased the activity, while MnCl2 and EDTA inhibited it. The enzyme catalyzed the hydrolysis of alpha 1-2, alpha 1-3, and alpha 1-6 mannosidic linkages.
authors.affiliation: Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hirata
authors.forename: Y
authors.initials: Y
authors.lastname: Aso
authors.forename: M
authors.initials: M
authors.lastname: Ishiguro
mesh_terms: D000818:Animals; D002236:Carbohydrate Conformation; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification*; D008361:Mannosidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012908:Snails / Q000201:enzymology*; D013379:Substrate Specificity; D043323:alpha-Mannosidase