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Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli

European Journal of Biochemistry

Dec 15, 1975

Claude LazdunskiA M Lazdunski

PMID: 1271

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Abstract

A periplasmic aminoendopeptidase from Escherichia coli has been purified to hemogeneity. It is a monomer of molecular weight 45000 and containing one -- SH group that is necessary for catalytic activity. The study of its substrate specificity indicated that the enzyme has both aminopept...read more

Mentioned in this Paper

Thermodynamics
Structure-Activity Relationship
Casein allergenic extract
Enzyme Activation
Protein Conformation
Sulfhydryl Compounds
Alanine
Hydrogen-Ion Concentration
Periplasm
Calorimetry
Paper Details
References
    • References4
    • Citations13
    • References4
    • Citations13
  • Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli

    European Journal of Biochemistry

    Dec 15, 1975

    Claude LazdunskiA M Lazdunski

    PMID: 1271

    DOI:

    Abstract

    A periplasmic aminoendopeptidase from Escherichia coli has been purified to hemogeneity. It is a monomer of molecular weight 45000 and containing one -- SH group that is necessary for catalytic activity. The study of its substrate specificity indicated that the enzyme has both aminopept...read more

    Mentioned in this Paper

    Thermodynamics
    Structure-Activity Relationship
    Casein allergenic extract
    Enzyme Activation
    Protein Conformation

    Related Papers

    Paper Details
    References
    • References4
    • Citations13
    • References4
    • Citations13
  • Get paper from

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