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Purification and properties of potato 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-(1,4-alpha-glucano)-transferase. Evidence against a dual catalytic function in amylose-branching enzyme

European Journal of Biochemistry

Nov 15, 1975

D BorovskyWilliam J Whelan

PMID: 1258

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Abstract

Q-Enzyme, the enzyme that synthesizes the 1,6-alpha-glucosidic branch linkages of amylopectin, has been purified from potato to near homogeneity. The molecular weight of the enzyme is 85000. The active enzyme is a monomer, with a molar activity at pH 7.0 and 24 degrees C of 15. The ener...read more

Mentioned in this Paper

Thermodynamics
Glycogen Branching Enzyme
Protein Conformation
Chloromercuribenzoates
Amylose
Hydrogen-Ion Concentration
Glucosyltransferases
Calorimetry
Plasma Protein Binding Capacity
Magnesium
Paper Details
References
    • References16
    • Citations10
    • References16
    • Citations10
  • Purification and properties of potato 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-(1,4-alpha-glucano)-transferase. Evidence against a dual catalytic function in amylose-branching enzyme

    European Journal of Biochemistry

    Nov 15, 1975

    D BorovskyWilliam J Whelan

    PMID: 1258

    DOI:

    Abstract

    Q-Enzyme, the enzyme that synthesizes the 1,6-alpha-glucosidic branch linkages of amylopectin, has been purified from potato to near homogeneity. The molecular weight of the enzyme is 85000. The active enzyme is a monomer, with a molar activity at pH 7.0 and 24 degrees C of 15. The ener...read more

    Mentioned in this Paper

    Thermodynamics
    Glycogen Branching Enzyme
    Protein Conformation
    Chloromercuribenzoates
    Amylose

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    Paper Details
    References
    • References16
    • Citations10
    • References16
    • Citations10
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