Comparative study of free and membrane-bound acidic beta-D-glucosidase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea: decapoda).

N N Chuang, J D Huang, K S Lin
Author Information
  1. N N Chuang: Division of Biochemistry and Molecular Science, Institute of Zoology, Academia Sinica, Nankang, Taipei,Republic of China.

Abstract

l. In the hepatopancreas of the shrimp Penaeus japonicus the beta-glucosidase is present, either free or membrane-bound. The specific activity of the purified enzyme is 237,333 units/mg of protein and 191,111 units/mg of protein for the free and the membrane-bound beta-glucosidase, respectively. 2.The non-membrane-bound beta-glucosidase appears to be the same molecular size as the membrane-bound enzyme, both being monomers and consisting of a polypeptide chain of apparent M(r) 65,000, as estimated by chromatography on Superose 12 and by SDS-PAGE. 3.Both enzymes share similarities in their molecular size and substrate specificities (with ratios of 100:17:4:12 for the non-membrane-bound and 100:32:13:12 for the membrane-bound enzyme for the activities with methylumbelliferyl-beta-D-glucoside, methylumbelliferyl-beta-D-galactoside, methylumbelliferyl-alpha -L-arabinopyranoside and methylumbelliferyl-beta-xyloside respectively, as substrates). 4.The membrane-bound beta-glucosidase can be differentiated from the non-membrane-bound enzyme by its isoelectric point (7.5 vs 6.6), Km (182 micrometer vs 76 micrometer), pH optimum (4.5 vs 5.5), phosphorylation,sialyation and thermostability.

MeSH Term

Animals
Electrophoresis, Polyacrylamide Gel
Hepatopancreas
Hot Temperature
Hydrogen-Ion Concentration
Isoelectric Focusing
Membrane Proteins
Molecular Weight
Penaeidae
Phosphorylation
Substrate Specificity
Time Factors
beta-Glucosidase

Chemicals

Membrane Proteins
beta-Glucosidase

Word Cloud

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