Prolyl carboxypeptidase purified from human placenta: its characterization and identification as an apelin-cleaving enzyme

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Prolyl carboxypeptidase purified from human placenta: its characterization and identification as an apelin-cleaving enzyme

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作者：Kaat Kehoe^a ; ^{kaat.kehoe@uantwerpen.be" class="auth_mail" title="E-mail the corresponding author} ; Roos Van Elzen^a ; Robert Verkerk^a ; Yani Sim^a ; Pieter Van der Veken^b ; Anne-Marie Lambeir^a ; Ingrid De Meester^a
关键词：α-MSH ; α-melanocyte-stimulating hormone ; ACE2 ; angiotensin-converting enzyme 2 ; Ala ; alanine ; Phe ; phenylalanine ; hPRCP ; purified human prolyl carboxypeptidase ; HUVECs ; human umbilical vein endothelial cells ; ITC ; isothermal titration calorimetry ; Pro ; proline ; PRCP ; prolyl carboxypeptidase ; (pyr)-apelin-13 ; pyroglutamated apelin-13 ; rhPRCP ; recombinant human prolyl carboxypeptidase ; Val ; valine ; Z ; N-benzyloxycarbonyl
刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
出版年：2016
出版时间：November 2016
年：2016
卷：1864
期：11
页码：1481-1488
全文大小：508 K

文摘

•: PRCP was purified from human placental tissue.
•: Purified PRCP has similar substrate specificity as recombinant PRCP.
•: Purified and recombinant PRCP hydrolyze (pyr)-apelin-13, apelin-17 and apelin-36.
•: Enterostatin, ghrelin and obestatin were not cleaved by purified and recombinant PRCP.

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