<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Goc A</submitter><funding>NEI NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>12409-19</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2645919</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>47(47)</volume><pubmed_abstract>Visual signal transduction serves as one of the best understood G protein-coupled receptor signaling systems. Signaling is initiated when a photon strikes rhodopsin (Rho) causing a conformational change leading to productive interaction of this G protein-coupled receptor with the heterotrimeric G protein, transducin (Gt). Here we describe a new method for Gt purification from native bovine rod photoreceptor membranes without subunit dissociation caused by exposure to photoactivated rhodopsin (Rho*). Native electrophoresis followed by immunoblotting revealed that Gt purified by this method formed more stable heterotrimers and interacted more efficiently with membranes containing Rho* or its target, phosphodiesterase 6, than did Gt purified by a traditional method involving subunit dissociat</pubmed_abstract><journal>Biochemistry</journal><pubmed_title>Different properties of the native and reconstituted heterotrimeric G protein transducin.</pubmed_title><pmcid>PMC2645919</pmcid><funding_grant_id>GM079191</funding_grant_id><funding_grant_id>P30 EY11373</funding_grant_id><funding_grant_id>P30 EY011373</funding_grant_id><funding_grant_id>R01 EY008061</funding_grant_id><funding_grant_id>EY008061</funding_grant_id><funding_grant_id>R01 GM079191</funding_grant_id><funding_grant_id>P30 EY011373-129005</funding_grant_id><funding_grant_id>R01 EY008061-22</funding_grant_id><funding_grant_id>R01 GM079191-02</funding_grant_id><funding_grant_id>T32 EY007157</funding_grant_id><pubmed_authors>Goc A</pubmed_authors><pubmed_authors>Palczewski K</pubmed_authors><pubmed_authors>Wang B</pubmed_authors><pubmed_authors>Jastrzebska B</pubmed_authors><pubmed_authors>Angel TE</pubmed_authors><pubmed_authors>Wintrode PL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Different properties of the native and reconstituted heterotrimeric G protein transducin.</name><description>Visual signal transduction serves as one of the best understood G protein-coupled receptor signaling systems. Signaling is initiated when a photon strikes rhodopsin (Rho) causing a conformational change leading to productive interaction of this G protein-coupled receptor with the heterotrimeric G protein, transducin (Gt). Here we describe a new method for Gt purification from native bovine rod photoreceptor membranes without subunit dissociation caused by exposure to photoactivated rhodopsin (Rho*). Native electrophoresis followed by immunoblotting revealed that Gt purified by this method formed more stable heterotrimers and interacted more efficiently with membranes containing Rho* or its target, phosphodiesterase 6, than did Gt purified by a traditional method involving subunit dissociat</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Nov</publication><modification>2025-04-04T07:58:30.842Z</modification><creation>2019-03-27T00:20:50Z</creation></dates><accession>S-EPMC2645919</accession><cross_references><pubmed>18975915</pubmed><doi>10.1021/bi8015444</doi></cross_references></HashMap>