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. 1982 Feb;149(2):515–522. doi: 10.1128/jb.149.2.515-522.1982

Purification of a soluble and a wall-bound form of beta-glucosidase from Mucor racemosus.

P I Borgia, D W Mehnert
PMCID: PMC216536  PMID: 6173375

Abstract

beta-Glucosidase activity in crude extracts of Mucor racemosus exists in a soluble form and in a wall-bound form which sediments at 3,500 x g. The soluble form and a wall-bound form were purified to homogeneity by ammonium sulfate fractionation. DEAE-Sephadex chromatography, and SP-Sephadex chromatography. Both forms were identical in all parameters measured. Each enzyme is a glycoprotein of 91,000 daltons, with an identical amino acid composition and N-terminal amino acid of lysine; both contain about 10% carbohydrate. Both forms catalyze the hydrolysis of cellobiose and p-nitrophenyl-beta-D-glucoside with identical kinetic constants.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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