Separation, purification, comparative properties and subcellular localization of acid and neutral alpha-D-mannosidase of monkey brain
Mathur, R.; Balasubramanian, A.S.
Indian Journal of Biochemistry and Biophysics 18(5): 334-341
1981
ISSN/ISBN: 0301-1208 PMID: 7341412 Document Number: 181565
The acid and neutral .alpha.-D-mannosidases of monkey brain were separated from each other by concanavalin A-Sepharose affinity chromatography and purified to apparent homogeniety. The thermal stability of the neutral enzyme in the presence of Co2+ ions was taken advantage of in the purification of this enzyme. The acid and neutral enzymes differed from each other in their binding characteristics to concanavalin A-Sepharose, pH optima profile, metal ion activation, thermal stability, Km, MW and subcellular localization. The acid enzyme was localized in the lysosomal and the neutral enzyme in the cytosolic fractions of monkey brain. Co2+ ions had both an activating as well as stabilizing effect on the neutral .alpha.-D-mannosidase.