Vmax. activation of pp60c-src tyrosine kinase from neuroblastoma neuro-2A
A kinetic analysis of the tyrosine-specific protein kinase of pp60c-src from the C1300 mouse neuroblastoma cell line Neuro-2A and pp60c-src expressed in fibroblasts was carried out to determine the nature of the increased specific activity of the neuroblastoma enzyme. In immune-complex kinase assays...
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| Veröffentlicht in: | Biochemical journal 1987-12, Vol.248 (3), p.691-696 |
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| creator | Matten, W T Maness, P F |
| description | A kinetic analysis of the tyrosine-specific protein kinase of pp60c-src from the C1300 mouse neuroblastoma cell line Neuro-2A and pp60c-src expressed in fibroblasts was carried out to determine the nature of the increased specific activity of the neuroblastoma enzyme. In immune-complex kinase assays with ATP-Mn2+ and the tyrosine-containing peptide angiotensin I as phosphoacceptor substrate, pp60c-src from the neuroblastoma cell line was characterized by a maximum velocity (Vmax.) that was 7-15-fold greater than the Vmax. of pp60c-src from fibroblasts. The neuroblastoma enzyme exhibited Km values for ATP (16 +/- 3 microM) and angiotensin I (6.8 +/- 2.6 mM) that were similar to Km values for ATP (25 +/- 3 microM) and angiotensin I (6.5 +/- 1.7 mM) of pp60c-src from fibroblasts. pp60v-src expressed in Rous-sarcoma-virus-transformed cells exhibited an ATP Km value (25 +/- 4 microM) and an angiotensin I Km value (6.6 +/- 0.5 mM) that approximated the values determined for pp60c-src in neuroblastoma cells and fibroblasts. These results indicate that the pp60c-src kinase from neuroblastoma cells has a higher turnover number than pp60c-src kinase from fibroblasts, and that the neural form of the enzyme would be expected to exhibit increased catalytic activity at the saturating concentrations of ATP that are found intracellularly. |
| doi_str_mv | 10.1042/bj2480691 |
| format | Article |
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In immune-complex kinase assays with ATP-Mn2+ and the tyrosine-containing peptide angiotensin I as phosphoacceptor substrate, pp60c-src from the neuroblastoma cell line was characterized by a maximum velocity (Vmax.) that was 7-15-fold greater than the Vmax. of pp60c-src from fibroblasts. The neuroblastoma enzyme exhibited Km values for ATP (16 +/- 3 microM) and angiotensin I (6.8 +/- 2.6 mM) that were similar to Km values for ATP (25 +/- 3 microM) and angiotensin I (6.5 +/- 1.7 mM) of pp60c-src from fibroblasts. pp60v-src expressed in Rous-sarcoma-virus-transformed cells exhibited an ATP Km value (25 +/- 4 microM) and an angiotensin I Km value (6.6 +/- 0.5 mM) that approximated the values determined for pp60c-src in neuroblastoma cells and fibroblasts. These results indicate that the pp60c-src kinase from neuroblastoma cells has a higher turnover number than pp60c-src kinase from fibroblasts, and that the neural form of the enzyme would be expected to exhibit increased catalytic activity at the saturating concentrations of ATP that are found intracellularly.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2480691</identifier><identifier>PMID: 3325040</identifier><language>eng</language><publisher>England</publisher><subject>Adenosine Triphosphate - pharmacokinetics ; Angiotensin I - pharmacokinetics ; Animals ; Cell Line ; Enzyme Activation ; Fibroblasts - enzymology ; Immunoelectrophoresis ; Kinetics ; Mice ; Neuroblastoma - metabolism ; Protein-Tyrosine Kinases - metabolism ; Proto-Oncogene Proteins - metabolism ; Tumor Cells, Cultured - metabolism</subject><ispartof>Biochemical journal, 1987-12, Vol.248 (3), p.691-696</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1148604/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1148604/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3325040$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matten, W T</creatorcontrib><creatorcontrib>Maness, P F</creatorcontrib><title>Vmax. activation of pp60c-src tyrosine kinase from neuroblastoma neuro-2A</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>A kinetic analysis of the tyrosine-specific protein kinase of pp60c-src from the C1300 mouse neuroblastoma cell line Neuro-2A and pp60c-src expressed in fibroblasts was carried out to determine the nature of the increased specific activity of the neuroblastoma enzyme. In immune-complex kinase assays with ATP-Mn2+ and the tyrosine-containing peptide angiotensin I as phosphoacceptor substrate, pp60c-src from the neuroblastoma cell line was characterized by a maximum velocity (Vmax.) that was 7-15-fold greater than the Vmax. of pp60c-src from fibroblasts. The neuroblastoma enzyme exhibited Km values for ATP (16 +/- 3 microM) and angiotensin I (6.8 +/- 2.6 mM) that were similar to Km values for ATP (25 +/- 3 microM) and angiotensin I (6.5 +/- 1.7 mM) of pp60c-src from fibroblasts. pp60v-src expressed in Rous-sarcoma-virus-transformed cells exhibited an ATP Km value (25 +/- 4 microM) and an angiotensin I Km value (6.6 +/- 0.5 mM) that approximated the values determined for pp60c-src in neuroblastoma cells and fibroblasts. These results indicate that the pp60c-src kinase from neuroblastoma cells has a higher turnover number than pp60c-src kinase from fibroblasts, and that the neural form of the enzyme would be expected to exhibit increased catalytic activity at the saturating concentrations of ATP that are found intracellularly.</description><subject>Adenosine Triphosphate - pharmacokinetics</subject><subject>Angiotensin I - pharmacokinetics</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Enzyme Activation</subject><subject>Fibroblasts - enzymology</subject><subject>Immunoelectrophoresis</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Neuroblastoma - metabolism</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Tumor Cells, Cultured - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1Lw0AQhhdRaq0e_AFCTt5SdzezH7kIRfwoFLyo1zBJdnVrko27SbH_3kKL6GlmeF-eB4aQS0bnjAK_KdccNJU5OyJTBoqmWnF9TKaUS0gl5eyUnMW4ppQBBTohkyzjYrdNyfKtxe95gtXgNjg43yXeJn0vaZXGUCXDNvjoOpN8ug6jSWzwbdKZMfiywTj4FvdXyhfn5MRiE83FYc7I68P9y91Tunp-XN4tVmnPJRtSW4tcoUJdlyC00NQKI5gReaWYVgozYUvIKMvQSiVVpaFGkAYgh7LOhc1m5HbP7ceyNXVluiFgU_TBtRi2hUdX_E8691G8-03BGGhJYQe4PgCC_xpNHIrWxco0DXbGj7FQKgfOlNgVr_6afhWH52U_EbtwkA</recordid><startdate>19871215</startdate><enddate>19871215</enddate><creator>Matten, W T</creator><creator>Maness, P F</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19871215</creationdate><title>Vmax. activation of pp60c-src tyrosine kinase from neuroblastoma neuro-2A</title><author>Matten, W T ; Maness, P F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p261t-fd597a7a8db458580f5e51e59c71877a35fb43013af6767c84da46e4494bd95f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Adenosine Triphosphate - pharmacokinetics</topic><topic>Angiotensin I - pharmacokinetics</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Enzyme Activation</topic><topic>Fibroblasts - enzymology</topic><topic>Immunoelectrophoresis</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Neuroblastoma - metabolism</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Tumor Cells, Cultured - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matten, W T</creatorcontrib><creatorcontrib>Maness, P F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matten, W T</au><au>Maness, P F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vmax. activation of pp60c-src tyrosine kinase from neuroblastoma neuro-2A</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1987-12-15</date><risdate>1987</risdate><volume>248</volume><issue>3</issue><spage>691</spage><epage>696</epage><pages>691-696</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>A kinetic analysis of the tyrosine-specific protein kinase of pp60c-src from the C1300 mouse neuroblastoma cell line Neuro-2A and pp60c-src expressed in fibroblasts was carried out to determine the nature of the increased specific activity of the neuroblastoma enzyme. In immune-complex kinase assays with ATP-Mn2+ and the tyrosine-containing peptide angiotensin I as phosphoacceptor substrate, pp60c-src from the neuroblastoma cell line was characterized by a maximum velocity (Vmax.) that was 7-15-fold greater than the Vmax. of pp60c-src from fibroblasts. The neuroblastoma enzyme exhibited Km values for ATP (16 +/- 3 microM) and angiotensin I (6.8 +/- 2.6 mM) that were similar to Km values for ATP (25 +/- 3 microM) and angiotensin I (6.5 +/- 1.7 mM) of pp60c-src from fibroblasts. pp60v-src expressed in Rous-sarcoma-virus-transformed cells exhibited an ATP Km value (25 +/- 4 microM) and an angiotensin I Km value (6.6 +/- 0.5 mM) that approximated the values determined for pp60c-src in neuroblastoma cells and fibroblasts. These results indicate that the pp60c-src kinase from neuroblastoma cells has a higher turnover number than pp60c-src kinase from fibroblasts, and that the neural form of the enzyme would be expected to exhibit increased catalytic activity at the saturating concentrations of ATP that are found intracellularly.</abstract><cop>England</cop><pmid>3325040</pmid><doi>10.1042/bj2480691</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1987-12, Vol.248 (3), p.691-696 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - pharmacokinetics Angiotensin I - pharmacokinetics Animals Cell Line Enzyme Activation Fibroblasts - enzymology Immunoelectrophoresis Kinetics Mice Neuroblastoma - metabolism Protein-Tyrosine Kinases - metabolism Proto-Oncogene Proteins - metabolism Tumor Cells, Cultured - metabolism |
| title | Vmax. activation of pp60c-src tyrosine kinase from neuroblastoma neuro-2A |
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