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Purification and specificity of prolyl dipeptidase from bovine kidney

Biochimica Et Biophysica Acta

Jan 23, 1976

A F Akrawi, George S Bailey

PMID: 2303

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Abstract

Prolyl dipeptidase (iminodipeptidase, L-prolyl-amino acid hydrolase, EC 3.4.13.8) was purified 180-fold from bovine kidney. The enzyme which was obtained in a 10% yield was completely separated from a number of known kidney peptidases including an enzyme of very similar substrate specif...read more

Mentioned in this Paper

Dipeptidases
Metazoa
Proline
Structure-Activity Relationship
Hydrogen-Ion Concentration
Kidney
Bos indicus
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  • Purification and specificity of prolyl dipeptidase from bovine kidney

    Biochimica Et Biophysica Acta

    Jan 23, 1976

    A F Akrawi, George S Bailey

    PMID: 2303

    DOI:

    Abstract

    Prolyl dipeptidase (iminodipeptidase, L-prolyl-amino acid hydrolase, EC 3.4.13.8) was purified 180-fold from bovine kidney. The enzyme which was obtained in a 10% yield was completely separated from a number of known kidney peptidases including an enzyme of very similar substrate specif...read more

    Mentioned in this Paper

    Dipeptidases
    Metazoa
    Proline
    Structure-Activity Relationship
    Hydrogen-Ion Concentration

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