Characterization of a distinct membrane bound dipeptidyl carboxypeptidase inactivating enkephalin in brain
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Co-identity of brain angiotensin converting enzyme with a membrane bound dipeptidyl carboxypeptidase inactivating Met-enkephalin
2. Two distinct enkephalinases: Solubilization, partial purification and separation from angiotensin converting enzyme
3. Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase
4. ‘Enkephalinase’ is distinct from brain ‘angiostensin-converting enzyme’
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1. A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11;Life Sciences;1993-01
2. Hydrolysis of angiotensin I by peptidases in homogenates of rat lung and aorta;Biochemical Pharmacology;1988-03
3. Prodynorphin processing by rat CNS fractions and purified enzymes: Formation of Dynorphin A 1–8 by sulfhydryl-activated carboxypeptidase and peptidyl dipeptidase;Neurochemistry International;1987-01
4. Synthesis and biological evaluation of phosphonamidate peptide inhibitors of enkephalinase and angiotensin-converting enzyme;Journal of Medicinal Chemistry;1985-09
5. Enkephalinase from rat kidney. Purification, characterization, and study of substrate specificity.;Journal of Biological Chemistry;1984-12
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