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

Charles Gorenstein, Solomon H Snyder

Research output: Contribution to journalArticle

Abstract

We have examined enkephalin degradation by solubilized membrane fractions of rat brain. Three distinct enkephalin degrading activities can be partially purified and chromatographically resolved. Aminopeptidase activity gives rise to free tyr, an enzyme designated enkephalinase A generates tyr-gly-gly while a newly reported enzyme activity, enkephalinase B, produces the tyr-gly fragment. Enkephalinase A activity can be completely resolved by DEAE column chromatography from angiotensin converting enzyme activity. This finding, together with a differential sensitivity of angiotensin converting enzyme and enkephalinase A activity to various reagents and salts, demonstrates that they are distinct enzymes.

Original languageEnglish (US)
Pages (from-to)2065-2070
Number of pages6
JournalLife Sciences
Volume25
Issue number24-25
DOIs
StatePublished - 1979

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Neprilysin
Peptidyl-Dipeptidase A
Purification
Enkephalins
Enzyme activity
tyrosyl-glycyl-glycine
Enzymes
Column chromatography
Aminopeptidases
Chromatography
Rats
Brain
Salts
Membranes
Degradation

ASJC Scopus subject areas

  • Pharmacology

Cite this

Two distinct enkephalinases : Solubilization, partial purification and separation from angiotensin converting enzyme. / Gorenstein, Charles; Snyder, Solomon H.

In: Life Sciences, Vol. 25, No. 24-25, 1979, p. 2065-2070.

Research output: Contribution to journalArticle

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