Asp. niger a-glucosidase wascrystallized in ammonium sulfate solution after chromatographies on DEAE-Sepharose CL-6Band TOYOPEARL HW-55columns. The crystalline a-glucosidase, which was a glycoprotein containing 25.5% carbohydrate as glucose, gave a single band on polyacrylamide disc gel electrophoresis. The molecular weight was estimated to be about 12.5 x 104 by SDS-disc gel electrophoresis. However, the crystalline enzyme consists of two components (M.W. about 3.3 x 104 and 9.8 x 104, respectively) separable only by reverse-phase HPLCcausing irreversible inactivation. The optimumpH was 4.3. The enzymealso hydrolyzed a-glucans such as soluble starch and amylose. The analyses of the primary structure and the catalytic groups of the crystalline a-glucosidase are under way in our laboratory. This paper describes the crystallization, the substrate specificity, and the subsite affinities of Asp. niger a-glucosidase.

No abstract

No abstract

No abstract

ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.