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

Charles Gorenstein; Solomon H. Snyder

doi:10.1016/0024-3205(79)90198-X

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

Charles Gorenstein, Solomon H. Snyder

School of Medicine

Research output: Contribution to journal › Article › peer-review

165 Scopus citations

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 language	English (US)
Pages (from-to)	2065-2070
Number of pages	6
Journal	Life Sciences
Volume	25
Issue number	24-25
DOIs	https://doi.org/10.1016/0024-3205(79)90198-X
State	Published - 1979

ASJC Scopus subject areas

General Pharmacology, Toxicology and Pharmaceutics
General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/0024-3205(79)90198-X

Cite this

@article{a44e875ed4ad440f8523a89197c759d3,

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

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.",

author = "Charles Gorenstein and Snyder, {Solomon H.}",

note = "Funding Information: Though distinct enzyme species, ACE and enkephalinase A have certain similarities, both appear to be metalloenzymes and both are susceptible to dithiothreitol, indicating the presence of a critical S-S bond or binding of a heavy metal co-factor by free aulfhydryl groups . The paradoxical stimulation of ACE activity by PMSF, which inhibits enkephalinase A, might be the result of stabilization of ACE against contaminating tissue proteasee . Acknowledgements We are grateful to Marls Bowman and Robert Horlick for their technical assistance sad to Dawn C. Hanks for manuscript preparation. Supported by USPHS grant DA0026 and grants of the Hartford and McRnight foundations .",

year = "1979",

doi = "10.1016/0024-3205(79)90198-X",

language = "English (US)",

volume = "25",

pages = "2065--2070",

journal = "Life Sciences",

issn = "0024-3205",

publisher = "Elsevier Inc.",

number = "24-25",

}

TY - JOUR

T1 - Two distinct enkephalinases

T2 - Solubilization, partial purification and separation from angiotensin converting enzyme

AU - Gorenstein, Charles

AU - Snyder, Solomon H.

N1 - Funding Information: Though distinct enzyme species, ACE and enkephalinase A have certain similarities, both appear to be metalloenzymes and both are susceptible to dithiothreitol, indicating the presence of a critical S-S bond or binding of a heavy metal co-factor by free aulfhydryl groups . The paradoxical stimulation of ACE activity by PMSF, which inhibits enkephalinase A, might be the result of stabilization of ACE against contaminating tissue proteasee . Acknowledgements We are grateful to Marls Bowman and Robert Horlick for their technical assistance sad to Dawn C. Hanks for manuscript preparation. Supported by USPHS grant DA0026 and grants of the Hartford and McRnight foundations .

PY - 1979

Y1 - 1979

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0018574789&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018574789&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(79)90198-X

DO - 10.1016/0024-3205(79)90198-X

M3 - Article

C2 - 231717

AN - SCOPUS:0018574789

SN - 0024-3205

VL - 25

SP - 2065

EP - 2070

JO - Life Sciences

JF - Life Sciences

IS - 24-25

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this