The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids
Recoverin is a recently identified Ca(2+)-binding protein that imparts Ca2+ sensitivity to vertebrate photoreceptor guanylate cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP. Bovine retinal recoverin has now been analyzed by el...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-08, Vol.267 (23), p.16033-16036 |
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| container_end_page | 16036 |
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| container_issue | 23 |
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| container_title | The Journal of biological chemistry |
| container_volume | 267 |
| creator | DIZHOOR, A. M ERICSSON, L. H JOHNSON, R. S KUMAR, S OLSHEVSKAYA, E ZOZULYA, S NEUBER, T. A STRYER, L HURLEY, J. B WALSH, K. A |
| description | Recoverin is a recently identified Ca(2+)-binding protein that imparts Ca2+ sensitivity to vertebrate photoreceptor guanylate
cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP.
Bovine retinal recoverin has now been analyzed by electrospray mass spectrometry (ESI-MS) for post-translational modifications
that might influence its activity. Heterogeneous acylation was detected at the NH2 terminus of bovine retinal recoverin. The
NH2-terminal glycine of each retinal recoverin molecule is linked to one of four different types of acyl groups. The most
abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present. |
| doi_str_mv | 10.1016/S0021-9258(18)41959-X |
| format | Article |
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cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP.
Bovine retinal recoverin has now been analyzed by electrospray mass spectrometry (ESI-MS) for post-translational modifications
that might influence its activity. Heterogeneous acylation was detected at the NH2 terminus of bovine retinal recoverin. The
NH2-terminal glycine of each retinal recoverin molecule is linked to one of four different types of acyl groups. The most
abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)41959-X</identifier><identifier>PMID: 1386601</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Acylation ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; Calcium-Binding Proteins - isolation & purification ; Calcium-Binding Proteins - metabolism ; Cattle ; Chromatography, Gas ; Eye Proteins ; Fundamental and applied biological sciences. Psychology ; Hippocalcin ; Lipoproteins ; Mass Spectrometry ; Molecular Sequence Data ; Molecular Weight ; Myristic Acid ; Myristic Acids - metabolism ; Nerve Tissue Proteins ; Peptide Fragments - isolation & purification ; Proteins ; Recombinant Proteins - metabolism ; Recoverin ; Rod Cell Outer Segment - metabolism ; Trypsin</subject><ispartof>The Journal of biological chemistry, 1992-08, Vol.267 (23), p.16033-16036</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-a54c5ab65a78c735535b8e7017ed24bc581ecff73bbe93e8169095f3db41ac6f3</citedby><cites>FETCH-LOGICAL-c409t-a54c5ab65a78c735535b8e7017ed24bc581ecff73bbe93e8169095f3db41ac6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5566531$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1386601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DIZHOOR, A. M</creatorcontrib><creatorcontrib>ERICSSON, L. H</creatorcontrib><creatorcontrib>JOHNSON, R. S</creatorcontrib><creatorcontrib>KUMAR, S</creatorcontrib><creatorcontrib>OLSHEVSKAYA, E</creatorcontrib><creatorcontrib>ZOZULYA, S</creatorcontrib><creatorcontrib>NEUBER, T. A</creatorcontrib><creatorcontrib>STRYER, L</creatorcontrib><creatorcontrib>HURLEY, J. B</creatorcontrib><creatorcontrib>WALSH, K. A</creatorcontrib><title>The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Recoverin is a recently identified Ca(2+)-binding protein that imparts Ca2+ sensitivity to vertebrate photoreceptor guanylate
cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP.
Bovine retinal recoverin has now been analyzed by electrospray mass spectrometry (ESI-MS) for post-translational modifications
that might influence its activity. Heterogeneous acylation was detected at the NH2 terminus of bovine retinal recoverin. The
NH2-terminal glycine of each retinal recoverin molecule is linked to one of four different types of acyl groups. The most
abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present.</description><subject>Acylation</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - isolation & purification</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cattle</subject><subject>Chromatography, Gas</subject><subject>Eye Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hippocalcin</subject><subject>Lipoproteins</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Myristic Acid</subject><subject>Myristic Acids - metabolism</subject><subject>Nerve Tissue Proteins</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recoverin</subject><subject>Rod Cell Outer Segment - metabolism</subject><subject>Trypsin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkFFLHDEQx0Ox2KvtRxDyINI-rM1sNtnksYitBVGwFu4tJNlJL5Ldtcmect--e96hzsvAzO8_Az9CjoGdAQP57TdjNVS6FuoLqK8NaKGr5TuyAKZ4xQUsD8jiBflAPpZyz-ZqNBySQ-BKSgYLcnu3Qnp9WdMJcx-HdaFjoBmnONg0dz8-Yo4DjYVav0l2wo66DbW09DYlGmwf02YbCXaa5rmPXflE3gebCn7e9yPy58fF3flldXXz89f596vKN0xPlRWNF9ZJYVvlWy4EF05hy6DFrm6cFwrQh9By51BzVCA10yLwzjVgvQz8iJzu7j7k8d8ay2T6WDymZAcc18W0nGlQrZhBsQN9HkvJGMxDjr3NGwPMbF2aZ5dmK8qAMs8uzXLOHe8frF2P3WtqJ2_en-z3tnibQraDj-UFE0JKwd9gq_h39RQzGhdHv8Le1LI1NTcgGef8P407h5o</recordid><startdate>19920815</startdate><enddate>19920815</enddate><creator>DIZHOOR, A. 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Psychology</topic><topic>Hippocalcin</topic><topic>Lipoproteins</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Myristic Acid</topic><topic>Myristic Acids - metabolism</topic><topic>Nerve Tissue Proteins</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recoverin</topic><topic>Rod Cell Outer Segment - metabolism</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DIZHOOR, A. M</creatorcontrib><creatorcontrib>ERICSSON, L. H</creatorcontrib><creatorcontrib>JOHNSON, R. S</creatorcontrib><creatorcontrib>KUMAR, S</creatorcontrib><creatorcontrib>OLSHEVSKAYA, E</creatorcontrib><creatorcontrib>ZOZULYA, S</creatorcontrib><creatorcontrib>NEUBER, T. A</creatorcontrib><creatorcontrib>STRYER, L</creatorcontrib><creatorcontrib>HURLEY, J. 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A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-08-15</date><risdate>1992</risdate><volume>267</volume><issue>23</issue><spage>16033</spage><epage>16036</epage><pages>16033-16036</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Recoverin is a recently identified Ca(2+)-binding protein that imparts Ca2+ sensitivity to vertebrate photoreceptor guanylate
cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP.
Bovine retinal recoverin has now been analyzed by electrospray mass spectrometry (ESI-MS) for post-translational modifications
that might influence its activity. Heterogeneous acylation was detected at the NH2 terminus of bovine retinal recoverin. The
NH2-terminal glycine of each retinal recoverin molecule is linked to one of four different types of acyl groups. The most
abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1386601</pmid><doi>10.1016/S0021-9258(18)41959-X</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-08, Vol.267 (23), p.16033-16036 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acylation Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Cattle Chromatography, Gas Eye Proteins Fundamental and applied biological sciences. Psychology Hippocalcin Lipoproteins Mass Spectrometry Molecular Sequence Data Molecular Weight Myristic Acid Myristic Acids - metabolism Nerve Tissue Proteins Peptide Fragments - isolation & purification Proteins Recombinant Proteins - metabolism Recoverin Rod Cell Outer Segment - metabolism Trypsin |
| title | The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids |
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