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Purification and characterization of acidic alpha-D-mannosidase from the hepatopancreas of the shrimpPenaeus monodon (Crustacea: Decapoda)

✍ Scribed by Chuang, Nin-Nin ;Yang, Bei-Chia ;Lin, Kung-Shih

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
641 KB
Volume
261
Category
Article
ISSN
0022-104X

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✦ Synopsis

Abstract

Acidic alpha‐D‐mannosidase purified from the hepatopancreas of Penaeus monodon is pentameric, with a Mr 251,000 as estimated by size‐exclusion FPLC on a Superose^TM^ 12, and retains a hydrophobic domain, being stable to heating at 65°C for 1 h. The specific activity of the purified enzyme is 1,923 units/mg of protein. After polyacrylamide gel electrophoresis under denaturing conditions, the purified acidic alpha‐D‐mannosidase from shrimp was found to consist of a single homogeneous type of monomer of Mr 51,000. The purified enzyme has an isoelectric point of 4.4 ± 0.1 and becomes more alkaline after the removal of either sialic acid or phosphate groups. The apparent K~m~ value of alpha‐D‐mannosidase from shrimp hepatopancreas with 4‐methylumbelliferylalpha‐D‐mannopyranoside as substrate is 243 μM. © 1992 Wiley‐Liss, Inc.

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