Biochemical characterization of angiotensin-converting enzyme in human neuroblastoma tissue.
High activity of angiotensin-converting enzyme was demonstrated in human neuroblastoma tissue. This activity required the presence of chloride ion and was almost completely inhibited by a specific converting enzyme inhibitor captopril (10 nM), indicating that the activity measured is indeed angiotensin-converting enzyme. Furthermore, the biochemical features of the enzyme were closely similar to the well-known properties of human lung converting enzyme, such as molecular weight (290,000), optimum pH (8.0-8.5), the presence of glycoprotein residues, and dependence on chloride ion concentration. These results provide definitive evidence for the presence of true angiotensin-converting enzyme in human neuroblastoma tissue.
D000806:Angiotensin-Converting Enzyme Inhibitors; D002216:Captopril / Q000494:pharmacology; D002675:Child, Preschool; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007223:Infant; D008168:Lung / Q000201:enzymology; D008970:Molecular Weight; D009447:Neuroblastoma / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D012685:Sepharose / Q000031:analogs & derivatives
D000806:Angiotensin-Converting Enzyme Inhibitors; D011506:Proteins; C028326:concanavalin A-sepharose; D012685:Sepharose; D002216:Captopril; D007703:Peptidyl-Dipeptidase A