Phosphorylation of Synaptic Membranes
: In vivo and in vitro phosphorylation of synaptic membrane proteins were compared. In vivo phosphorylation was carried out by injecting rats intraventricularly with 1 mCi of 32Pi‐orthophosphate. After a 40‐min isotope incorporation period, rats were decapitated and synaptic membranes isolated. In v...
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| Veröffentlicht in: | Journal of neurochemistry 1980-02, Vol.34 (2), p.431-437 |
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| container_issue | 2 |
| container_start_page | 431 |
| container_title | Journal of neurochemistry |
| container_volume | 34 |
| creator | Berman, Robert F. Hullihan, John P. Kinnier, William J. Wilson, John Eric |
| description | :
In vivo and in vitro phosphorylation of synaptic membrane proteins were compared. In vivo phosphorylation was carried out by injecting rats intraventricularly with 1 mCi of 32Pi‐orthophosphate. After a 40‐min isotope incorporation period, rats were decapitated and synaptic membranes isolated. In vitro phosphorylation was accomplished by incubating unlabeled synaptic membranes, isolated from noninjected rats, with 5 μM‐[γ‐32P]ATP. In vivo and in vitro32P‐labeled synaptic membranes were then fractionated electrophoretically on an SDS‐polyacrylamide (7.5%) slab gel. The Coomassie blue protein patterns for in vivo and in vitro32P‐labeled synaptic membranes were identical. In contrast, autoradiographs of these gels showed striking differences in the pattern of phosphate incorporation. Cyclic‐AMP (10 μM) maximally stimulated) the in vitro phosphate labeling of two protein bands (80,000 and 55,000 apparent molecular weight) which were not substantially labeled by the in vivo procedure. |
| doi_str_mv | 10.1111/j.1471-4159.1980.tb06614.x |
| format | Article |
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In vivo and in vitro phosphorylation of synaptic membrane proteins were compared. In vivo phosphorylation was carried out by injecting rats intraventricularly with 1 mCi of 32Pi‐orthophosphate. After a 40‐min isotope incorporation period, rats were decapitated and synaptic membranes isolated. In vitro phosphorylation was accomplished by incubating unlabeled synaptic membranes, isolated from noninjected rats, with 5 μM‐[γ‐32P]ATP. In vivo and in vitro32P‐labeled synaptic membranes were then fractionated electrophoretically on an SDS‐polyacrylamide (7.5%) slab gel. The Coomassie blue protein patterns for in vivo and in vitro32P‐labeled synaptic membranes were identical. In contrast, autoradiographs of these gels showed striking differences in the pattern of phosphate incorporation. Cyclic‐AMP (10 μM) maximally stimulated) the in vitro phosphate labeling of two protein bands (80,000 and 55,000 apparent molecular weight) which were not substantially labeled by the in vivo procedure.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1111/j.1471-4159.1980.tb06614.x</identifier><identifier>PMID: 6251169</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Brain protein phosphorylation ; Cyclic AMP - metabolism ; Male ; Membrane protein phosphorylation ; Membrane Proteins - metabolism ; Molecular Weight ; Phosphorylation ; Protein phosphorylation in vivo ; Rats ; Synaptic membranes ; Synaptic Membranes - metabolism</subject><ispartof>Journal of neurochemistry, 1980-02, Vol.34 (2), p.431-437</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3691-bb978c74a712064ceb3840749d83e91187b9e8feb9a87eadea31114a93c201b63</citedby><cites>FETCH-LOGICAL-c3691-bb978c74a712064ceb3840749d83e91187b9e8feb9a87eadea31114a93c201b63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1471-4159.1980.tb06614.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1471-4159.1980.tb06614.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6251169$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berman, Robert F.</creatorcontrib><creatorcontrib>Hullihan, John P.</creatorcontrib><creatorcontrib>Kinnier, William J.</creatorcontrib><creatorcontrib>Wilson, John Eric</creatorcontrib><title>Phosphorylation of Synaptic Membranes</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>:
In vivo and in vitro phosphorylation of synaptic membrane proteins were compared. In vivo phosphorylation was carried out by injecting rats intraventricularly with 1 mCi of 32Pi‐orthophosphate. After a 40‐min isotope incorporation period, rats were decapitated and synaptic membranes isolated. In vitro phosphorylation was accomplished by incubating unlabeled synaptic membranes, isolated from noninjected rats, with 5 μM‐[γ‐32P]ATP. In vivo and in vitro32P‐labeled synaptic membranes were then fractionated electrophoretically on an SDS‐polyacrylamide (7.5%) slab gel. The Coomassie blue protein patterns for in vivo and in vitro32P‐labeled synaptic membranes were identical. In contrast, autoradiographs of these gels showed striking differences in the pattern of phosphate incorporation. Cyclic‐AMP (10 μM) maximally stimulated) the in vitro phosphate labeling of two protein bands (80,000 and 55,000 apparent molecular weight) which were not substantially labeled by the in vivo procedure.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Brain protein phosphorylation</subject><subject>Cyclic AMP - metabolism</subject><subject>Male</subject><subject>Membrane protein phosphorylation</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>Phosphorylation</subject><subject>Protein phosphorylation in vivo</subject><subject>Rats</subject><subject>Synaptic membranes</subject><subject>Synaptic Membranes - metabolism</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEtLw0AUhQdRaq3-BKEIukucOzOZhwtBik_qA9T1MJNOaErSiZkUm39vQkP33s1dnHPu40PoAnAMXV2vYmACIgaJikFJHDcWcw4s3h6g8V46RGOMCYkoZuQYnYSwwhg44zBCI04SAK7G6PJj6UO19HVbmCb366nPpp_t2lRNnk5fXWlrs3bhFB1lpgjubOgT9P1w_zV7iubvj8-zu3mUUq4gslYJmQpmBBDMWeoslQwLphaSOgUghVVOZs4qI4UzC2do9w4ziqYEg-V0gq52c6va_2xcaHSZh9QVRXeE3wQtEsKYSmRnvNkZ09qHULtMV3VemrrVgHXPSK90D0L3IHTPSA-M9LYLnw9bNrZ0i310gNLptzv9Ny9c-4_J-uVtxijQP5hrdVA</recordid><startdate>198002</startdate><enddate>198002</enddate><creator>Berman, Robert F.</creator><creator>Hullihan, John P.</creator><creator>Kinnier, William J.</creator><creator>Wilson, John Eric</creator><general>Blackwell Publishing Ltd</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>198002</creationdate><title>Phosphorylation of Synaptic Membranes</title><author>Berman, Robert F. ; Hullihan, John P. ; Kinnier, William J. ; Wilson, John Eric</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3691-bb978c74a712064ceb3840749d83e91187b9e8feb9a87eadea31114a93c201b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Brain protein phosphorylation</topic><topic>Cyclic AMP - metabolism</topic><topic>Male</topic><topic>Membrane protein phosphorylation</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>Phosphorylation</topic><topic>Protein phosphorylation in vivo</topic><topic>Rats</topic><topic>Synaptic membranes</topic><topic>Synaptic Membranes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berman, Robert F.</creatorcontrib><creatorcontrib>Hullihan, John P.</creatorcontrib><creatorcontrib>Kinnier, William J.</creatorcontrib><creatorcontrib>Wilson, John Eric</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>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berman, Robert F.</au><au>Hullihan, John P.</au><au>Kinnier, William J.</au><au>Wilson, John Eric</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of Synaptic Membranes</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1980-02</date><risdate>1980</risdate><volume>34</volume><issue>2</issue><spage>431</spage><epage>437</epage><pages>431-437</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><abstract>:
In vivo and in vitro phosphorylation of synaptic membrane proteins were compared. In vivo phosphorylation was carried out by injecting rats intraventricularly with 1 mCi of 32Pi‐orthophosphate. After a 40‐min isotope incorporation period, rats were decapitated and synaptic membranes isolated. In vitro phosphorylation was accomplished by incubating unlabeled synaptic membranes, isolated from noninjected rats, with 5 μM‐[γ‐32P]ATP. In vivo and in vitro32P‐labeled synaptic membranes were then fractionated electrophoretically on an SDS‐polyacrylamide (7.5%) slab gel. The Coomassie blue protein patterns for in vivo and in vitro32P‐labeled synaptic membranes were identical. In contrast, autoradiographs of these gels showed striking differences in the pattern of phosphate incorporation. Cyclic‐AMP (10 μM) maximally stimulated) the in vitro phosphate labeling of two protein bands (80,000 and 55,000 apparent molecular weight) which were not substantially labeled by the in vivo procedure.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>6251169</pmid><doi>10.1111/j.1471-4159.1980.tb06614.x</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of neurochemistry, 1980-02, Vol.34 (2), p.431-437 |
| issn | 0022-3042 1471-4159 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Adenosine Triphosphate - metabolism Animals Brain protein phosphorylation Cyclic AMP - metabolism Male Membrane protein phosphorylation Membrane Proteins - metabolism Molecular Weight Phosphorylation Protein phosphorylation in vivo Rats Synaptic membranes Synaptic Membranes - metabolism |
| title | Phosphorylation of Synaptic Membranes |
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