Prolyl carboxypeptidase purified from human placenta: its characterization and identification as an apelin-cleaving enzyme
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- 作者：Kaat Kehoea ; kaat.kehoe@uantwerpen.be" class="auth_mail" title="E-mail the corresponding author ; Roos Van Elzena ; Robert Verkerka ; Yani Sima ; Pieter Van der Vekenb ; Anne-Marie Lambeira ; Ingrid De Meestera
- 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
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PRCP was purified from human placental tissue.
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Purified PRCP has similar substrate specificity as recombinant PRCP.
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Purified and recombinant PRCP hydrolyze (pyr)-apelin-13, apelin-17 and apelin-36.
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Enterostatin, ghrelin and obestatin were not cleaved by purified and recombinant PRCP.