Enkephalin inactivation by N-terminal tyrosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain
A soluble enzyme which rapidly degrades both Met and Leu-enkephalin by cleavage of the Tyr-Gly bond has been identified in homogenates of corpora striata from human brain. A marked preference for Met-enkephalin as substrate over Leu-enkephalin was observed. Tyr was not cleaved from other closely rel...
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| Veröffentlicht in: | Life sciences (1973) 1980-05, Vol.26 (20), p.1697-1706 |
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| container_issue | 20 |
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| container_title | Life sciences (1973) |
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| creator | Traficante, Louis J. Rotrosen, John Siekierski, Joanne Tracer, Howard Gershon, Samuel |
| description | A soluble enzyme which rapidly degrades both Met and Leu-enkephalin by cleavage of the Tyr-Gly bond has been identified in homogenates of corpora striata from human brain. A marked preference for Met-enkephalin as substrate over Leu-enkephalin was observed. Tyr was not cleaved from other closely related peptides: these include Tyr-Gly-Gly, Tyr-Gly, γ-endorphin, and (d-Ala
2)-Met-enkephalin. Tyr cleavage is catalyzed by a labile, neutral, freeze-sensitive metalloenzyme that is nearly completely inhibited by zinc, bacitracin, puromycin, o-phenanthroline and γ-endorphin. 2-Mercaptoethanol was found to stabilize activity during purification and characterization. This enzyme was purified to homogeneity by chromatography on DEAE-Sephadex and Biogel A 1.5m, and determined to have an apparent molecular weight of 61,500 daltons by SDS-polyacrylamide gel electrophoresis. |
| doi_str_mv | 10.1016/0024-3205(80)90178-2 |
| format | Article |
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2)-Met-enkephalin. Tyr cleavage is catalyzed by a labile, neutral, freeze-sensitive metalloenzyme that is nearly completely inhibited by zinc, bacitracin, puromycin, o-phenanthroline and γ-endorphin. 2-Mercaptoethanol was found to stabilize activity during purification and characterization. This enzyme was purified to homogeneity by chromatography on DEAE-Sephadex and Biogel A 1.5m, and determined to have an apparent molecular weight of 61,500 daltons by SDS-polyacrylamide gel electrophoresis.</description><identifier>ISSN: 0024-3205</identifier><identifier>EISSN: 1879-0631</identifier><identifier>DOI: 10.1016/0024-3205(80)90178-2</identifier><identifier>PMID: 7392806</identifier><language>eng</language><publisher>Netherlands: Elsevier Inc</publisher><subject>Aminopeptidases - isolation & purification ; Aminopeptidases - metabolism ; Brain - enzymology ; Corpus Striatum - enzymology ; Electrophoresis, Polyacrylamide Gel ; Endorphins - metabolism ; Enkephalins - metabolism ; Humans ; Methionine - metabolism ; Molecular Weight ; Substrate Specificity ; Tyrosine - metabolism</subject><ispartof>Life sciences (1973), 1980-05, Vol.26 (20), p.1697-1706</ispartof><rights>1980</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-bd94264af1eb2d68f74f6c9128a596eaf31669630c5cf2aa850055f03b8a07af3</citedby><cites>FETCH-LOGICAL-c357t-bd94264af1eb2d68f74f6c9128a596eaf31669630c5cf2aa850055f03b8a07af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0024320580901782$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7392806$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Traficante, Louis J.</creatorcontrib><creatorcontrib>Rotrosen, John</creatorcontrib><creatorcontrib>Siekierski, Joanne</creatorcontrib><creatorcontrib>Tracer, Howard</creatorcontrib><creatorcontrib>Gershon, Samuel</creatorcontrib><title>Enkephalin inactivation by N-terminal tyrosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain</title><title>Life sciences (1973)</title><addtitle>Life Sci</addtitle><description>A soluble enzyme which rapidly degrades both Met and Leu-enkephalin by cleavage of the Tyr-Gly bond has been identified in homogenates of corpora striata from human brain. A marked preference for Met-enkephalin as substrate over Leu-enkephalin was observed. Tyr was not cleaved from other closely related peptides: these include Tyr-Gly-Gly, Tyr-Gly, γ-endorphin, and (d-Ala
2)-Met-enkephalin. Tyr cleavage is catalyzed by a labile, neutral, freeze-sensitive metalloenzyme that is nearly completely inhibited by zinc, bacitracin, puromycin, o-phenanthroline and γ-endorphin. 2-Mercaptoethanol was found to stabilize activity during purification and characterization. This enzyme was purified to homogeneity by chromatography on DEAE-Sephadex and Biogel A 1.5m, and determined to have an apparent molecular weight of 61,500 daltons by SDS-polyacrylamide gel electrophoresis.</description><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Brain - enzymology</subject><subject>Corpus Striatum - enzymology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endorphins - metabolism</subject><subject>Enkephalins - metabolism</subject><subject>Humans</subject><subject>Methionine - metabolism</subject><subject>Molecular Weight</subject><subject>Substrate Specificity</subject><subject>Tyrosine - metabolism</subject><issn>0024-3205</issn><issn>1879-0631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFu1TAQRS0EKq-FPwDJKwSLgO0kjsOiEqpaQKqABaytiTNuDIkT7ORJ6U_wyzjkqUtWlnzPvaO5Q8gLzt5yxuU7xkSR5YKVrxV7UzNeqUw8IgeuqjpjMuePyeEBeUrOY_zJGCvLKj8jZ1VeC8Xkgfy59r9w6qB3njoPZnZHmN3oabPSL9mMYUi_PZ3XMEbnkZoe4Qh3-J5-W4Kzzuw0-JZOEGaXWNNBSEEY3P0ujpYC7dxd1680Tmg2G0V_vw5IbRgH2i0DpIkBnH9GnljoIz4_vRfkx83196tP2e3Xj5-vPtxmJi-rOWvauhCyAMuxEa1UtiqsNDUXCspaIticS1nLnJnSWAGgym11y_JGAauSfEFe7blTGH8vGGc9uGiw78HjuERdlSlAFXUCix00qYEY0OopuAHCqjnT2x30VrLeStaK6X930CLZXp7yl2bA9sF0Kj7pl7uOacmjw6CjcegNti6gmXU7uv8P-AstRJot</recordid><startdate>19800519</startdate><enddate>19800519</enddate><creator>Traficante, Louis J.</creator><creator>Rotrosen, John</creator><creator>Siekierski, Joanne</creator><creator>Tracer, Howard</creator><creator>Gershon, Samuel</creator><general>Elsevier Inc</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>19800519</creationdate><title>Enkephalin inactivation by N-terminal tyrosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain</title><author>Traficante, Louis J. ; Rotrosen, John ; Siekierski, Joanne ; Tracer, Howard ; Gershon, Samuel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-bd94264af1eb2d68f74f6c9128a596eaf31669630c5cf2aa850055f03b8a07af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Brain - enzymology</topic><topic>Corpus Striatum - enzymology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endorphins - metabolism</topic><topic>Enkephalins - metabolism</topic><topic>Humans</topic><topic>Methionine - metabolism</topic><topic>Molecular Weight</topic><topic>Substrate Specificity</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Traficante, Louis J.</creatorcontrib><creatorcontrib>Rotrosen, John</creatorcontrib><creatorcontrib>Siekierski, Joanne</creatorcontrib><creatorcontrib>Tracer, Howard</creatorcontrib><creatorcontrib>Gershon, Samuel</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>Life sciences (1973)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Traficante, Louis J.</au><au>Rotrosen, John</au><au>Siekierski, Joanne</au><au>Tracer, Howard</au><au>Gershon, Samuel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enkephalin inactivation by N-terminal tyrosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain</atitle><jtitle>Life sciences (1973)</jtitle><addtitle>Life Sci</addtitle><date>1980-05-19</date><risdate>1980</risdate><volume>26</volume><issue>20</issue><spage>1697</spage><epage>1706</epage><pages>1697-1706</pages><issn>0024-3205</issn><eissn>1879-0631</eissn><abstract>A soluble enzyme which rapidly degrades both Met and Leu-enkephalin by cleavage of the Tyr-Gly bond has been identified in homogenates of corpora striata from human brain. A marked preference for Met-enkephalin as substrate over Leu-enkephalin was observed. Tyr was not cleaved from other closely related peptides: these include Tyr-Gly-Gly, Tyr-Gly, γ-endorphin, and (d-Ala
2)-Met-enkephalin. Tyr cleavage is catalyzed by a labile, neutral, freeze-sensitive metalloenzyme that is nearly completely inhibited by zinc, bacitracin, puromycin, o-phenanthroline and γ-endorphin. 2-Mercaptoethanol was found to stabilize activity during purification and characterization. This enzyme was purified to homogeneity by chromatography on DEAE-Sephadex and Biogel A 1.5m, and determined to have an apparent molecular weight of 61,500 daltons by SDS-polyacrylamide gel electrophoresis.</abstract><cop>Netherlands</cop><pub>Elsevier Inc</pub><pmid>7392806</pmid><doi>10.1016/0024-3205(80)90178-2</doi><tpages>10</tpages></addata></record> |
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| ispartof | Life sciences (1973), 1980-05, Vol.26 (20), p.1697-1706 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Aminopeptidases - isolation & purification Aminopeptidases - metabolism Brain - enzymology Corpus Striatum - enzymology Electrophoresis, Polyacrylamide Gel Endorphins - metabolism Enkephalins - metabolism Humans Methionine - metabolism Molecular Weight Substrate Specificity Tyrosine - metabolism |
| title | Enkephalin inactivation by N-terminal tyrosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain |
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