Angiotensin-Converting Enzyme, Enkephalinase a and Aminopeptidases in the Breakdown of Enkephalin - Studies in Cell Cultures

1984 ◽  
Vol 6 (10-11) ◽  
pp. 1829-1832 ◽  
Author(s):  
H. Lentzen ◽  
I. Reinsch ◽  
J. Linke
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Cell Cultures ◽  
Converting Enzyme ◽  
Enkephalinase A

Enkephalinases

1980 ◽  
Vol 210 (1178) ◽  
pp. 123-132 ◽  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Column Chromatography ◽  
Opiate Receptors ◽  
Converting Enzyme ◽  
Regional Variations ◽  
Amino Terminal ◽  
Brain Membranes ◽  
Enkephalinase A ◽  
Detergent Treatment ◽  
Deae Column

Enkephalins can be degraded by a variety of peptidases. We have chara­terized several membrane-associated brain peptidases in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin. We have distinguished two carboxyldirected dipeptidylpeptidases, designated enkephalinase A 1 and A 2 , that give rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations in enkephalinase A 1 activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A 1 has been purified 1500-fold, to appar­ent homogeneity.

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