Purification of some glycoside hydrolases by affinity chromatography

Michael Edward, Robert J. Sturgeon

    Research output: Contribution to journalArticle

    Abstract

    Two glycoproteins have been isolated from the cell walls of baker's yeast. One is a glucan-protein complex which has been partially characterised as having a branched carbohydrate structure composed of chains of (1?3)-linked ß-d-glucosyl residues, some of which are attached by (1?6)-linkages to the main chain. Immobilization of this glycoprotein was achieved by covalent attachment to Sepharose, and the product was used to isolate a number of (1?3)-ß-d-glucan hydrolases from Helix pomatia, malted barley, and Basidiomycete QM806. The second glycoprotein, a mannan-protein complex, after immobilization, has been used in the purification of an a-d-mannosidase from jack-bean meal. © 1977.

    Original languageEnglish
    Pages (from-to)3-13
    Number of pages11
    JournalCarbohydrate Research
    Volume57
    Issue numberC
    Publication statusPublished - Aug 1977

    Fingerprint

    Affinity chromatography
    Glycoside Hydrolases
    Purification
    Glycoproteins
    Glucans
    Mannosidases
    Mannans
    Jacks
    Hydrolases
    Yeast
    Sepharose
    Proteins
    Cells
    Carbohydrates

    Cite this

    Edward, Michael ; Sturgeon, Robert J. / Purification of some glycoside hydrolases by affinity chromatography. In: Carbohydrate Research. 1977 ; Vol. 57, No. C. pp. 3-13.
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    Edward, M & Sturgeon, RJ 1977, 'Purification of some glycoside hydrolases by affinity chromatography', Carbohydrate Research, vol. 57, no. C, pp. 3-13.

    Purification of some glycoside hydrolases by affinity chromatography. / Edward, Michael; Sturgeon, Robert J.

    In: Carbohydrate Research, Vol. 57, No. C, 08.1977, p. 3-13.

    Research output: Contribution to journalArticle

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