作者: Joseph J. Lanzillo , Yamuna Dasarathy , Joanne Stevens , Barry L. Fanburg
DOI: 10.1016/S0006-291X(86)80487-9
关键词: Carboxypeptidase 、 Bradykinin 、 Lisinopril 、 Kunitz STI protease inhibitor 、 Biochemistry 、 PMSF 、 Thiorphan 、 Phosphoramidon 、 Angiotensin-converting enzyme 、 Chemistry 、 Biophysics 、 Cell biology 、 Molecular biology
摘要: Cultured bovine pulmonary artery endothelial cells contain a second peptidyl dipeptidase, distinct from angiotensin-converting enzyme, present in an inactive form associated with non-dialyzable inhibitor. Partial purification by glycine affinity chromatography separates enzyme inhibitor to yield preparation which hydrolyzes angiotensin-1, bradykinin, substance P, atriopeptin-2, enkephalin and Hip-His-Leu. This is resistant inhibition lisinopril, captopril, thiorphan, phosphoramidon, soybean trypsin inhibitor, PMSF aminopeptidase carboxypeptidase inhibitors, but inhibited EDTA.