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Journal ArticleDOI

Two distinct enkephalinases: solubilization, partial purification and separation from angiotensin converting enzyme.

TLDR
Enkephalinase A activity can be completely resolved by DEAE column chromatography from angiotensin converting enzyme activity, demonstrating that they are distinct enzymes.
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This article is published in Life Sciences.The article was published on 1979-12-10. It has received 171 citations till now. The article focuses on the topics: Enkephalinase & Enzyme assay.

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Citations
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Journal ArticleDOI

The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice

TL;DR: Thiorphan is reported here that this compound, thiorphan [(DL-3-mercapto-2-benzylpropanoyl)-glycine; patent no. 8008601] protects the enkephalins from the action of enkephalinase in vitro in nanomolar concentration and in vivo after either intracerebroventricular or systemic administration.
Journal ArticleDOI

Brain peptides as neurotransmitters.

TL;DR: Peptides, such as cholecystokinin and vasoactive intestinal polypeptide, were known as intestinal hormones and later recognized as brain constituents and may also be central neurotransmitters.
Journal ArticleDOI

Biological inactivation of enkephalins and the role of enkephalin-dipeptidyl-carboxypeptidase ("enkephalinase") as neuropeptidase.

TL;DR: Three types of well defined peptidase activities in CNS may account for the hydrolysis of the opioid pentapeptides : aminopeptidases, angiotensin-converting enzyme and enkephalin-dipeptidylcarboxypeptidase.
Journal ArticleDOI

Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli

TL;DR: The endopeptidase is present in caudate synaptic membranes and could play an important role in the hydrolysis of neuropeptides and should be designated "endopePTidase-24".
Journal ArticleDOI

A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11

TL;DR: This review summarizes the physical characteristics and distribution of angiotensin converting enzyme (E.C. 3.4.15.1), a known Ang I processing enzyme, and compares its features to what is known of prolyl endopeptidase and neutral endopePTidase 24.24.11.
References
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Journal ArticleDOI

High-affinity enkephalin-degrading peptidase in brain is increased after morphine

TL;DR: The presence of a high-affinity peptidase in a particulate fraction of mouse striatum splitting the Leu-enkephalin molecule with release of a tripeptide fragment and exhibiting definite substrate specificity suggests that it might be associated with enkphalinergic transmission.
Journal ArticleDOI

Mode of deactivation of the enkephalins by rat and human plasma and rat brain homogenates.

TL;DR: Hughes et al.5 have shown that the opiate activity isolated by them is due to a mixture of two peptides H–Tyr–Gly– Gly–Phe–Met–OH and H-Tyr-Gly-Phe-Leu–OH termed methionine-enkephalin and leucine- enkephaline respectively.
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Distribution and properties of angiotensin converting enzyme of rat brain

TL;DR: The broad substrate specificity of the enzymes suggests that, in addition to the possible contribution of the enzyme to the brain renin‐angiotensin system, other naturally occurring peptides might also be substrates for the enzyme.
Journal ArticleDOI

Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase

TL;DR: The experiments indicate that rapid inactivation of enkephalins may be due to at least two different enzymes present in tissues.
Journal ArticleDOI

Enkephalin catabolism in vitro and in vivo.

TL;DR: The rapid metabolism of the enkephalins and related compounds should be prevented if meaningful assessments of relative potency are to be made.
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