A purified oligopeptidase from Treponema denticola hydrolyzed bonds at the carboxyl side of proline in oxytocin, as well as in several other human bioactive peptides.
In plain wordsIn lab tests, an enzyme from a mouth bacterium cut oxytocin and several other human peptides.
- Peptide
- Oxytocin
- Outcome
- Not applicableHydrolysis of oxytocin by bacterial prolyl oligopeptidase
- Study
n: not reported in source
Purified Treponema denticola prolyl oligopeptidase- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
The enzyme hydrolyzed (optimum pH 6.5) the Pro-pNA bond in carbobenzoxy-Gly-Pro-p-nitroanilide (Z-Gly-Pro-pNA) and bonds at the carboxyl side of proline in several human bioactive peptides, such as bradykinin, substance P, neurotensin, angiotensins, oxytocin, vasopressin, and human endothelin fragment 22-38.
In this study, Oxytocin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Oxytocin.