Literature DB >> 9972247

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

K Hirata1, Y Aso, M Ishiguro.   

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.

Entities:  

Mesh:

Substances:

Year:  1998        PMID: 9972247     DOI: 10.1271/bbb.62.2242

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  2 in total

1.  PROTEIN N-GLYCOSYLATION OF GASTROPODS.

Authors:  Erika Staudacher; Herwig Stepan; Martin Gutternigg
Journal:  Curr Top Biochem Res       Date:  2009-12

2.  Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization.

Authors:  Martín S Godoy; Alfredo Castro-Vazquez; Alfredo Castro-Vasquez; Israel A Vega
Journal:  PLoS One       Date:  2013-06-20       Impact factor: 3.240

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.