Properties of alpha-mannosidase partially purified from the apple snail, Pomacea canaliculata

Authors
Hirata, K Aso, Y Ishiguro, M
Citation
K. Hirata et al., Properties of alpha-mannosidase partially purified from the apple snail, Pomacea canaliculata, BIOS BIOT B, 62(11), 1998, pp. 2242-2245
Citations number
28
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
09168451 → ACNP
Volume
62
Issue
11
Year of publication
1998
Pages
2242 - 2245
Database
ISI
SICI code
0916-8451(199811)62:11<2242:POAPPF>2.0.ZU;2-H
Abstract
Pomacea canaliculata alpha-mannosidase (260 kDa), composed of at least two isoforms with different pI, was partially purified. The activity was maximu m 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.