Jan 23, 1976

Purification and specificity of prolyl dipeptidase from bovine kidney

Biochimica Et Biophysica Acta
A F Akrawi, G S Bailey

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 specificity, proline aminopeptidase (L-prolyl-peptide hydrolase, EC 3.4.11.5). The specific activity of the enzyme with L-prolylglycine as substrate is 1600 units of activity per mg protein. Optimum activity of the enzyme is at pH 8.75 and the molecular weight on gel filtration was estimated to be 100 000. The isoelectric point of the enzyme is pH 4.25. Studies of substrate specificity showed that the enzyme preferentially hydrolyzes dipeptides and dipeptidyl amides with L-proline or hydroxy-L-proline at the N-terminus. Longer chain substrates with N-terminal proline were not hydrolyzed.

  • References2
  • Citations3

References

Mentioned in this Paper

Structure-Activity Relationship
Kidney
Proline
Bos indicus
Dipeptidases
Hydrogen-Ion Concentration
Metazoa

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