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Properties of Partially Purified Goat Kidney beta-D-mannosidase

Properties of Partially Purified Goat Kidney beta-D-mannosidase

R D Pearce, J W Callahan, A Novak, P B Little, J T Clarke

Br Vet J. May-Jun 1990;146(3):270-80.

PMID: 2364260

Abstract:

Lysosomal beta-D-mannosidase (EC 3.2.1.25) was purified 6900-fold from normal goat kidney by serial Concanavalin A-Sepharose 4B and Red A dye ligand affinity chromatography, followed by anion exchange and molecular sieve high performance liquid chromatography. The relative molecular mass of the enzyme was estimated by molecular sieving to be 79,000 +/- 3000. The apparent Km for the synthetic substrate, 4-methylumbelliferyl-beta-D-mannopyranoside, was 2.3-2.8 mM and the sharp, unimodal pH optimum was 5.5. Enzyme activity was inhibited by Hg2+, Zn2+, Ag+, Co2+ and the thiol reactive agent N-ethylmaleimide. The mannose derivatives p-nitrophenyl-beta-D- thiomannopyranoside and p-aminophenyl-beta-D-thiomannopyranoside inhibited enzyme activity and may be of use as immobilized ligands in future attempts to purify beta-D-mannosidase by specific affinity chromatography.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP67909302	4-Methylumbelliferyl β-D-mannopyranoside		67909-30-2	Price

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