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

作者信息

Hirata K, Aso Y, Ishiguro M

机构信息

Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.

出版信息

Biosci Biotechnol Biochem. 1998 Nov;62(11):2242-5. doi: 10.1271/bbb.62.2242.

DOI:10.1271/bbb.62.2242
PMID:9972247
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.

摘要

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