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Purification, molecular multiplicity and kinetic properties of "biosynthetic" L-threonine dehydratase from E. coli K-12

Biokhimii︠a︡

Jan 1, 1975

I A DorozhkoZ S Kagan

PMID: 2333

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Abstract

"Biosynthetic" L-threonine dehydratase was purified to homogeneous state with yield 29% of total activity from E. coli K-12. The cells were disrupted by means of ultra sound. Nucleic acids and nucleoproteins were precipitated with protamine sulphate, the proteins were fractioned with (N...read more

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Threonine Dehydratase
Polyacrylamide Gels
Protamine Sulfate (USP)
Nucleic Acids
Sephadex G 25
DEAE-Cellulose
Electrophoresis
Hydrogen-Ion Concentration
Gel Chromatography
Purification Aspects
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  • Purification, molecular multiplicity and kinetic properties of "biosynthetic" L-threonine dehydratase from E. coli K-12

    Biokhimii︠a︡

    Jan 1, 1975

    I A DorozhkoZ S Kagan

    PMID: 2333

    DOI:

    Abstract

    "Biosynthetic" L-threonine dehydratase was purified to homogeneous state with yield 29% of total activity from E. coli K-12. The cells were disrupted by means of ultra sound. Nucleic acids and nucleoproteins were precipitated with protamine sulphate, the proteins were fractioned with (N...read more

    Mentioned in this Paper

    Threonine Dehydratase
    Polyacrylamide Gels
    Protamine Sulfate (USP)
    Nucleic Acids
    Sephadex G 25

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    Paper Details
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