In a cell-free lamb-brain enzyme preparation, post-proline cleaving enzyme catalyzed oxytocin hydrolysis at the carboxyl side of proline residues.
In plain wordsIn lab tests, the lamb-brain enzyme broke down oxytocin at sites beside proline residues.
- Peptide
- Oxytocin
- Outcome
- DecreaseOxytocin hydrolysis by post-proline cleaving enzyme
- Study
lambn: not reported in source
Purified lamb-brain post-proline cleaving enzyme- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
The enzyme was most active at pH 7.0 with carbobenzoxy-Gly-Pro-beta-naphthylamide (Z-Gly-Pro-2-NNap) as a substrate and catalyzed the hydrolysis of oxytocin, vasopressin, thyrotropin releasing hormone (TRH), substance P, luteinizing hormone releasing hormone (LH-RH), and angiotensin at the carboxyl…
1 context sentence(design, population, supporting numbers)
A post-proline cleaving enzyme [post-proline endopeptidase: EC 3.4.21.26] was purified from lamb brain by a series of column chromatographies on DEAE-Sephadex, hydroxyapatite and Sephadex G-150. The purified enzyme appeared homogeneous on disc gel and sodium dodecyl sulfate (SDS) gel electrophoreses.
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.