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Bovine procarboxypeptidase A: kinetics of peptide and ester hydrolysis

Biochemistry

Feb 24, 1976

T J Bazzone, Bert L Vallee

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Abstract

Bovine procarboxypeptidase A exhibits intrinsic hydrolytic activity toward haloacyl amino acids (Behnke and Vallee, 1972), as well as toward conventional peptide and ester substrates for carboxypeptidase A (Bezzone, 1974; Uren and Neurath, 1974). The kinetics of hydrolysis of a series o...read more

Mentioned in this Paper

Hydrolysis
Metazoa
Catalysis
Metabolic Inhibition
Structure-Activity Relationship
Enzyme Activation
Bos taurus
Cattle
Hydrogen-Ion Concentration
Carboxypeptidase A Activity
Paper Details
References
    • References24
    • Citations4
    • References24
    • Citations4
  • Bovine procarboxypeptidase A: kinetics of peptide and ester hydrolysis

    Biochemistry

    Feb 24, 1976

    T J Bazzone, Bert L Vallee

    PMID: 2289

    DOI: 10.1021/bi00649a022

    Abstract

    Bovine procarboxypeptidase A exhibits intrinsic hydrolytic activity toward haloacyl amino acids (Behnke and Vallee, 1972), as well as toward conventional peptide and ester substrates for carboxypeptidase A (Bezzone, 1974; Uren and Neurath, 1974). The kinetics of hydrolysis of a series o...read more

    Mentioned in this Paper

    Hydrolysis
    Metazoa
    Catalysis
    Metabolic Inhibition
    Structure-Activity Relationship

    Related Papers

    Paper Details
    References
    • References24
    • Citations4
    • References24
    • Citations4
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