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Enkephalinases
Enkephalins can be degraded by a variety of peptidases. We have characterized several membrane-associated brain peptidases in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin. We have distinguished two carboxyl-directed dipepti...
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| Published in: | Proceedings of the Royal Society of London. Series B, Biological sciences Biological sciences, 1980-10, Vol.210 (1178), p.123-132 |
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| Main Authors: | , |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c559t-b2c834d2679e1d77f2300409f9ed7b9283c9edb5ee52a947ed51c2483dc102ea3 |
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| container_end_page | 132 |
| container_issue | 1178 |
| container_start_page | 123 |
| container_title | Proceedings of the Royal Society of London. Series B, Biological sciences |
| container_volume | 210 |
| creator | Gorenstein, C. Snyder, S. H. |
| description | Enkephalins can be degraded by a variety of peptidases. We have characterized several membrane-associated brain peptidases
in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin.
We have distinguished two carboxyl-directed dipeptidylpeptidases, designated enkephalinase A$_{1}$ and A$_{2}$, that give
rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations
in enkephalinase A$_{1}$ activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase
B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from
brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A$_{1}$
has been purified 1500-fold, to apparent homogeneity. |
| doi_str_mv | 10.1098/rspb.1980.0123 |
| format | article |
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in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin.
We have distinguished two carboxyl-directed dipeptidylpeptidases, designated enkephalinase A$_{1}$ and A$_{2}$, that give
rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations
in enkephalinase A$_{1}$ activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase
B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from
brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A$_{1}$
has been purified 1500-fold, to apparent homogeneity.</description><identifier>ISSN: 0962-8452</identifier><identifier>ISSN: 0080-4649</identifier><identifier>ISSN: 0950-1193</identifier><identifier>EISSN: 1471-2954</identifier><identifier>EISSN: 2053-9193</identifier><identifier>DOI: 10.1098/rspb.1980.0123</identifier><identifier>PMID: 6107926</identifier><language>eng</language><publisher>London: The Royal Society</publisher><subject>Aminopeptidases - metabolism ; Animals ; Brain - enzymology ; Brain Mapping ; Chromatography ; Corpus striatum ; Electrophoresis ; Endorphins - metabolism ; Enkephalins - metabolism ; Enzymes ; Gels ; Lectins ; Lentils ; Male ; Molecules ; Neurotransmitters ; Opioid receptors ; Peptide Hydrolases - isolation & purification ; Peptide Hydrolases - metabolism ; Rats ; Substrate Specificity</subject><ispartof>Proceedings of the Royal Society of London. Series B, Biological sciences, 1980-10, Vol.210 (1178), p.123-132</ispartof><rights>Copyright 1980 The Royal Society</rights><rights>Scanned images copyright © 2017, Royal Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c559t-b2c834d2679e1d77f2300409f9ed7b9283c9edb5ee52a947ed51c2483dc102ea3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/35421$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/35421$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,58216,58449</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6107926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gorenstein, C.</creatorcontrib><creatorcontrib>Snyder, S. H.</creatorcontrib><title>Enkephalinases</title><title>Proceedings of the Royal Society of London. Series B, Biological sciences</title><addtitle>Proc. R. Soc. Lond. B</addtitle><addtitle>Proc R Soc Lond B Biol Sci</addtitle><description>Enkephalins can be degraded by a variety of peptidases. We have characterized several membrane-associated brain peptidases
in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin.
We have distinguished two carboxyl-directed dipeptidylpeptidases, designated enkephalinase A$_{1}$ and A$_{2}$, that give
rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations
in enkephalinase A$_{1}$ activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase
B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from
brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A$_{1}$
has been purified 1500-fold, to apparent homogeneity.</description><subject>Aminopeptidases - metabolism</subject><subject>Animals</subject><subject>Brain - enzymology</subject><subject>Brain Mapping</subject><subject>Chromatography</subject><subject>Corpus striatum</subject><subject>Electrophoresis</subject><subject>Endorphins - metabolism</subject><subject>Enkephalins - metabolism</subject><subject>Enzymes</subject><subject>Gels</subject><subject>Lectins</subject><subject>Lentils</subject><subject>Male</subject><subject>Molecules</subject><subject>Neurotransmitters</subject><subject>Opioid receptors</subject><subject>Peptide Hydrolases - isolation & purification</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Rats</subject><subject>Substrate Specificity</subject><issn>0962-8452</issn><issn>0080-4649</issn><issn>0950-1193</issn><issn>1471-2954</issn><issn>2053-9193</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNp9UEtv1DAQthCobAscOSBx5ZbF40dsnxCtWkCqBOJxHiXOhPWSTYKdgJZfT7JZVVoherJH32vmY-w58DVwZ1_H1JdrcJavOQj5gK1AGciE0-ohW3GXi8wqLR6z85S2nHOnrT5jZzlw40S-Ys-u2x_Ub4omtEWi9IQ9qosm0dPje8G-3Vx_vXqf3X589-Hq7W3mtXZDVgpvpapEbhxBZUwtJOeKu9pRZUonrPTTr9REWhROGao0eKGsrDxwQYW8YK8W3z52P0dKA-5C8tQ0RUvdmNBoKXKnYCKuF6KPXUqRauxj2BVxj8BxLgDnAnAuAOcCJsHLo_NY7qi6ox8vnnC54LHbTxd2PtCwx203xnYa_--a7lN9_vLpEpx2vwTwAGAsciuBKymlxj-hP9jNBJwIGFIaCQ-005h_U18sqds0dPHuFKmVmJuBBdyE75vfIRKe7DYNfUzlIfAQtRi-uVczx_uuHagdToRYj02DfVXLv0QavCg</recordid><startdate>19801029</startdate><enddate>19801029</enddate><creator>Gorenstein, C.</creator><creator>Snyder, S. H.</creator><general>The Royal Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19801029</creationdate><title>Enkephalinases</title><author>Gorenstein, C. ; Snyder, S. H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c559t-b2c834d2679e1d77f2300409f9ed7b9283c9edb5ee52a947ed51c2483dc102ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Aminopeptidases - metabolism</topic><topic>Animals</topic><topic>Brain - enzymology</topic><topic>Brain Mapping</topic><topic>Chromatography</topic><topic>Corpus striatum</topic><topic>Electrophoresis</topic><topic>Endorphins - metabolism</topic><topic>Enkephalins - metabolism</topic><topic>Enzymes</topic><topic>Gels</topic><topic>Lectins</topic><topic>Lentils</topic><topic>Male</topic><topic>Molecules</topic><topic>Neurotransmitters</topic><topic>Opioid receptors</topic><topic>Peptide Hydrolases - isolation & purification</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Rats</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gorenstein, C.</creatorcontrib><creatorcontrib>Snyder, S. H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Proceedings of the Royal Society of London. Series B, Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gorenstein, C.</au><au>Snyder, S. H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enkephalinases</atitle><jtitle>Proceedings of the Royal Society of London. Series B, Biological sciences</jtitle><stitle>Proc. R. Soc. Lond. B</stitle><addtitle>Proc R Soc Lond B Biol Sci</addtitle><date>1980-10-29</date><risdate>1980</risdate><volume>210</volume><issue>1178</issue><spage>123</spage><epage>132</epage><pages>123-132</pages><issn>0962-8452</issn><issn>0080-4649</issn><issn>0950-1193</issn><eissn>1471-2954</eissn><eissn>2053-9193</eissn><abstract>Enkephalins can be degraded by a variety of peptidases. We have characterized several membrane-associated brain peptidases
in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin.
We have distinguished two carboxyl-directed dipeptidylpeptidases, designated enkephalinase A$_{1}$ and A$_{2}$, that give
rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations
in enkephalinase A$_{1}$ activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase
B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from
brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A$_{1}$
has been purified 1500-fold, to apparent homogeneity.</abstract><cop>London</cop><pub>The Royal Society</pub><pmid>6107926</pmid><doi>10.1098/rspb.1980.0123</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 0962-8452 |
| ispartof | Proceedings of the Royal Society of London. Series B, Biological sciences, 1980-10, Vol.210 (1178), p.123-132 |
| issn | 0962-8452 0080-4649 0950-1193 1471-2954 2053-9193 |
| language | eng |
| recordid | cdi_royalsociety_journals_10_1098_rspb_1980_0123 |
| source | JSTOR; Royal Society Publishing Jisc Collections Royal Society Journals Read & Publish Transitional Agreement 2025 (reading list) |
| subjects | Aminopeptidases - metabolism Animals Brain - enzymology Brain Mapping Chromatography Corpus striatum Electrophoresis Endorphins - metabolism Enkephalins - metabolism Enzymes Gels Lectins Lentils Male Molecules Neurotransmitters Opioid receptors Peptide Hydrolases - isolation & purification Peptide Hydrolases - metabolism Rats Substrate Specificity |
| title | Enkephalinases |
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