Degradation of α and β neo-endorphin by rat brain membrane peptidases

Charles Ulrich; Louis B. Hersh

doi:10.1016/0196-9781(85)90113-5

Degradation of α and β neo-endorphin by rat brain membrane peptidases

Charles Ulrich
, Louis B. Hersh

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

15 Scopus citations

Abstract

Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze β-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, α-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on β-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.

Original language	English
Pages (from-to)	475-482
Number of pages	8
Journal	Peptides
Volume	6
Issue number	3
DOIs	https://doi.org/10.1016/0196-9781(85)90113-5
State	Published - 1985

Bibliographical note

Funding Information:
The technical assistance of Ms. Vicki Choate is gratefully acknowledged. Charles Ulrich is a recipient of a Chilton Foundation fellowship. This research was supported in part by Grant No. DA-02243 from N1DA and Grant No. 1-131 from the Robert A. Welch Foundation, Houston, Texas.

Funding

The technical assistance of Ms. Vicki Choate is gratefully acknowledged. Charles Ulrich is a recipient of a Chilton Foundation fellowship. This research was supported in part by Grant No. DA-02243 from N1DA and Grant No. 1-131 from the Robert A. Welch Foundation, Houston, Texas.

Funders	Funder number
Chilton Foundation	1-131, DA-02243
National Institute on Drug Abuse	R01DA002243
Welch Foundation

Keywords

Aminopeptidase
Angiotensin converting enzyme
Neo-endorphins
Opioid peptide degradation

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/0196-9781(85)90113-5

Cite this

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title = "Degradation of α and β neo-endorphin by rat brain membrane peptidases",

abstract = "Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze β-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, α-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on β-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.",

keywords = "Aminopeptidase, Angiotensin converting enzyme, Neo-endorphins, Opioid peptide degradation",

author = "Charles Ulrich and Hersh, \{Louis B.\}",

note = "Funding Information: The technical assistance of Ms. Vicki Choate is gratefully acknowledged. Charles Ulrich is a recipient of a Chilton Foundation fellowship. This research was supported in part by Grant No. DA-02243 from N1DA and Grant No. 1-131 from the Robert A. Welch Foundation, Houston, Texas.",

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language = "English",

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pages = "475--482",

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T1 - Degradation of α and β neo-endorphin by rat brain membrane peptidases

AU - Ulrich, Charles

AU - Hersh, Louis B.

N1 - Funding Information: The technical assistance of Ms. Vicki Choate is gratefully acknowledged. Charles Ulrich is a recipient of a Chilton Foundation fellowship. This research was supported in part by Grant No. DA-02243 from N1DA and Grant No. 1-131 from the Robert A. Welch Foundation, Houston, Texas.

PY - 1985

Y1 - 1985

N2 - Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze β-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, α-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on β-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.

AB - Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze β-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, α-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on β-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.

KW - Aminopeptidase

KW - Angiotensin converting enzyme

KW - Neo-endorphins

KW - Opioid peptide degradation

UR - https://www.scopus.com/pages/publications/0022245187

UR - https://www.scopus.com/pages/publications/0022245187#tab=citedBy

U2 - 10.1016/0196-9781(85)90113-5

DO - 10.1016/0196-9781(85)90113-5

M3 - Article

C2 - 2999726

AN - SCOPUS:0022245187

SN - 0196-9781

VL - 6

SP - 475

EP - 482

JO - Peptides

JF - Peptides

IS - 3

ER -

Degradation of α and β neo-endorphin by rat brain membrane peptidases

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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