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Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADPglucose:1,4-alpha-D-glucan 4-alpha-glucosyltransferase

Biochemistry

Feb 24, 1976

James Martin FoxJack Preiss

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Abstract

The Escherichia coli B glycogen synthase has been purified to apparent homogeneity with the use of a 4-aminobutyl-Sepharose column. Two fractions of the enzyme were obtained: glycogen synthase I with a specific activity of 380 mumol mg-1 and devoid of branching enzyme activity and glyco...read more

Mentioned in this Paper

Glycogen Synthase I
Gluconolactone
Enzymes, antithrombotic
Syncope
Branching Enzyme Activity
Enzymes, peripheral vasodilators
Amylases
Maltodextrin
Genetic Linkage
Enzymes, hematological
Paper Details
References
    • References19
    • Citations27
    • References19
    • Citations27
  • Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADPglucose:1,4-alpha-D-glucan 4-alpha-glucosyltransferase

    Biochemistry

    Feb 24, 1976

    James Martin FoxJack Preiss

    PMID: 2288

    DOI: 10.1021/bi00649a019

    Abstract

    The Escherichia coli B glycogen synthase has been purified to apparent homogeneity with the use of a 4-aminobutyl-Sepharose column. Two fractions of the enzyme were obtained: glycogen synthase I with a specific activity of 380 mumol mg-1 and devoid of branching enzyme activity and glyco...read more

    Mentioned in this Paper

    Glycogen Synthase I
    Gluconolactone
    Enzymes, antithrombotic
    Syncope
    Branching Enzyme Activity

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    Paper Details
    References
    • References19
    • Citations27
    • References19
    • Citations27
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