Reversal of Rous Sarcoma-Specific Immunoglobulin Phosphorylation on Tyrosine (ADP as Phosphate Acceptor) Catalyzed by the src Gene Kinase
To determine the equilibrium constant of the reaction between ATP and protein-bound tyrosine we used as catalyst the highly purified Rous sarcoma src gene transcript. J. M. Sturtevant had earlier found (personal communication) that free tyrosine O-phosphate, upon hydrolysis with alkaline phosphatase...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1983-04, Vol.80 (7), p.1872-1876 |
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| container_end_page | 1876 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Fukami, Yasuo Lipmann, Fritz |
| description | To determine the equilibrium constant of the reaction between ATP and protein-bound tyrosine we used as catalyst the highly purified Rous sarcoma src gene transcript. J. M. Sturtevant had earlier found (personal communication) that free tyrosine O-phosphate, upon hydrolysis with alkaline phosphatase in a calorimeter (37 degrees C, pH 9), yielded a Δ H degrees of -2.8 kcal/mol (1 kcal = 4.18 kJ), less than half of that found in ATP hydrolysis. Experience with protein-bound serine phosphate (in phosvitin) had shown it to be energy rich [Rabinowitz, M. & Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050]. We wondered if the same is true for tyrosine phosphate when it is protein bound. From the equilibrium constant of 2.62 (at pH 6.5 and 5 mM Mg2+), we calculate a Δ G degrees′of -9.48 kcal/mol for hydrolysis of protein-bound tyrosine phosphate, assuming an approximate Δ G degrees′of -10 kcal/mol for hydrolysis of ATP. The experiments show that protein-bound tyrosine phosphate is energy rich, like serine phosphate in phosvitin. |
| doi_str_mv | 10.1073/pnas.80.7.1872 |
| format | Article |
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J. M. Sturtevant had earlier found (personal communication) that free tyrosine O-phosphate, upon hydrolysis with alkaline phosphatase in a calorimeter (37 degrees C, pH 9), yielded a Δ H degrees of -2.8 kcal/mol (1 kcal = 4.18 kJ), less than half of that found in ATP hydrolysis. Experience with protein-bound serine phosphate (in phosvitin) had shown it to be energy rich [Rabinowitz, M. & Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050]. We wondered if the same is true for tyrosine phosphate when it is protein bound. From the equilibrium constant of 2.62 (at pH 6.5 and 5 mM Mg2+), we calculate a Δ G degrees′of -9.48 kcal/mol for hydrolysis of protein-bound tyrosine phosphate, assuming an approximate Δ G degrees′of -10 kcal/mol for hydrolysis of ATP. The experiments show that protein-bound tyrosine phosphate is energy rich, like serine phosphate in phosvitin.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.80.7.1872</identifier><identifier>PMID: 6188157</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenosine Diphosphate - metabolism ; Animals ; Avian Sarcoma Viruses - enzymology ; Biochemistry ; Enzymes ; Free energy ; Gels ; Hydrolysis ; Immunoglobulin G - metabolism ; Kinetics ; Oncogene Protein pp60(v-src) ; Phosphatases ; Phosphates ; Phosphorylation ; Phosphotyrosine ; Protein Kinases - metabolism ; Rabbits ; Radioactive decay ; Rous sarcoma virus ; src genes ; Thermodynamics ; Tyrosine - analogs & derivatives ; Tyrosine - metabolism ; Viral Proteins - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1983-04, Vol.80 (7), p.1872-1876</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c487t-b721d2a58ee4cd34bcf9da405e8f8c02ea8eb6f1964d194d1f313022fe6d131a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/80/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/13395$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/13395$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6188157$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukami, Yasuo</creatorcontrib><creatorcontrib>Lipmann, Fritz</creatorcontrib><title>Reversal of Rous Sarcoma-Specific Immunoglobulin Phosphorylation on Tyrosine (ADP as Phosphate Acceptor) Catalyzed by the src Gene Kinase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>To determine the equilibrium constant of the reaction between ATP and protein-bound tyrosine we used as catalyst the highly purified Rous sarcoma src gene transcript. J. M. Sturtevant had earlier found (personal communication) that free tyrosine O-phosphate, upon hydrolysis with alkaline phosphatase in a calorimeter (37 degrees C, pH 9), yielded a Δ H degrees of -2.8 kcal/mol (1 kcal = 4.18 kJ), less than half of that found in ATP hydrolysis. Experience with protein-bound serine phosphate (in phosvitin) had shown it to be energy rich [Rabinowitz, M. & Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050]. We wondered if the same is true for tyrosine phosphate when it is protein bound. From the equilibrium constant of 2.62 (at pH 6.5 and 5 mM Mg2+), we calculate a Δ G degrees′of -9.48 kcal/mol for hydrolysis of protein-bound tyrosine phosphate, assuming an approximate Δ G degrees′of -10 kcal/mol for hydrolysis of ATP. The experiments show that protein-bound tyrosine phosphate is energy rich, like serine phosphate in phosvitin.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Animals</subject><subject>Avian Sarcoma Viruses - enzymology</subject><subject>Biochemistry</subject><subject>Enzymes</subject><subject>Free energy</subject><subject>Gels</subject><subject>Hydrolysis</subject><subject>Immunoglobulin G - metabolism</subject><subject>Kinetics</subject><subject>Oncogene Protein pp60(v-src)</subject><subject>Phosphatases</subject><subject>Phosphates</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine</subject><subject>Protein Kinases - metabolism</subject><subject>Rabbits</subject><subject>Radioactive decay</subject><subject>Rous sarcoma virus</subject><subject>src genes</subject><subject>Thermodynamics</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - metabolism</subject><subject>Viral Proteins - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS0EKkvhygEJyacKDlns2ImdA4fVAqWiElVbzpbjjLupnDi1k4rwD_jXeLVLWS4geeTD-95oZh5CLylZUiLYu6HXcSnJUiypFPkjtKCkolnJK_IYLQjJRSZ5zp-iZzHeEkKqQpIjdFRSKWkhFujnJdxDiNphb_GlnyK-0sH4TmdXA5jWtgafdd3U-xvn68m1Pb7Y-DhsfJidHlvf4_Su5-Bj2wN-s_pwgXXcM3oEvDIGhtGHt3itR-3mH9DgesbjBnAMBp9Ccn1p0w7wHD2x2kV4sf-P0bdPH6_Xn7Pzr6dn69V5ZrgUY1aLnDa5LiQANw3jtbFVozkpQFppSA5aQl1aWpW8oVUqyygjeW6hbCijmh2j97u-w1R30Bjox6CdGkLb6TArr1v1t9K3G3Xj7xWrmKB58p_s_cHfTRBH1bXRgHO6h3Q_JQlnhFflf0HKCiHzkidwuQNNOmMMYB-GoURtQ1bbkFNjJdQ25GR4fbjCA75P9UDf-n6rh_6Tf-nKTs6N8H1M4KsdeBtThn_GYqwq2C-nksbH</recordid><startdate>19830401</startdate><enddate>19830401</enddate><creator>Fukami, Yasuo</creator><creator>Lipmann, Fritz</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7T5</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19830401</creationdate><title>Reversal of Rous Sarcoma-Specific Immunoglobulin Phosphorylation on Tyrosine (ADP as Phosphate Acceptor) Catalyzed by the src Gene Kinase</title><author>Fukami, Yasuo ; Lipmann, Fritz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-b721d2a58ee4cd34bcf9da405e8f8c02ea8eb6f1964d194d1f313022fe6d131a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Animals</topic><topic>Avian Sarcoma Viruses - enzymology</topic><topic>Biochemistry</topic><topic>Enzymes</topic><topic>Free energy</topic><topic>Gels</topic><topic>Hydrolysis</topic><topic>Immunoglobulin G - metabolism</topic><topic>Kinetics</topic><topic>Oncogene Protein pp60(v-src)</topic><topic>Phosphatases</topic><topic>Phosphates</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine</topic><topic>Protein Kinases - metabolism</topic><topic>Rabbits</topic><topic>Radioactive decay</topic><topic>Rous sarcoma virus</topic><topic>src genes</topic><topic>Thermodynamics</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - metabolism</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukami, Yasuo</creatorcontrib><creatorcontrib>Lipmann, Fritz</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukami, Yasuo</au><au>Lipmann, Fritz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reversal of Rous Sarcoma-Specific Immunoglobulin Phosphorylation on Tyrosine (ADP as Phosphate Acceptor) Catalyzed by the src Gene Kinase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1983-04-01</date><risdate>1983</risdate><volume>80</volume><issue>7</issue><spage>1872</spage><epage>1876</epage><pages>1872-1876</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>To determine the equilibrium constant of the reaction between ATP and protein-bound tyrosine we used as catalyst the highly purified Rous sarcoma src gene transcript. J. M. Sturtevant had earlier found (personal communication) that free tyrosine O-phosphate, upon hydrolysis with alkaline phosphatase in a calorimeter (37 degrees C, pH 9), yielded a Δ H degrees of -2.8 kcal/mol (1 kcal = 4.18 kJ), less than half of that found in ATP hydrolysis. Experience with protein-bound serine phosphate (in phosvitin) had shown it to be energy rich [Rabinowitz, M. & Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050]. We wondered if the same is true for tyrosine phosphate when it is protein bound. From the equilibrium constant of 2.62 (at pH 6.5 and 5 mM Mg2+), we calculate a Δ G degrees′of -9.48 kcal/mol for hydrolysis of protein-bound tyrosine phosphate, assuming an approximate Δ G degrees′of -10 kcal/mol for hydrolysis of ATP. The experiments show that protein-bound tyrosine phosphate is energy rich, like serine phosphate in phosvitin.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6188157</pmid><doi>10.1073/pnas.80.7.1872</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Diphosphate - metabolism Animals Avian Sarcoma Viruses - enzymology Biochemistry Enzymes Free energy Gels Hydrolysis Immunoglobulin G - metabolism Kinetics Oncogene Protein pp60(v-src) Phosphatases Phosphates Phosphorylation Phosphotyrosine Protein Kinases - metabolism Rabbits Radioactive decay Rous sarcoma virus src genes Thermodynamics Tyrosine - analogs & derivatives Tyrosine - metabolism Viral Proteins - metabolism |
| title | Reversal of Rous Sarcoma-Specific Immunoglobulin Phosphorylation on Tyrosine (ADP as Phosphate Acceptor) Catalyzed by the src Gene Kinase |
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