Chromatographic Resolution and Kinetic Characterization of Glucokinase from Islets of Langerhans
Glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) from rat islets of Langerhans was partially purified by chromatography on DEAE-Cibacron blue F3GA agarose. The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for bo...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1983-01, Vol.80 (1), p.85-89 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Meglasson, Martin D. Burch, Pamela Trueheart Berner, Donna K. Najafi, Habiba Vogin, Alan P. Matschinsky, Franz M. |
| description | Glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) from rat islets of Langerhans was partially purified by chromatography on DEAE-Cibacron blue F3GA agarose. The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for both enzyme fraction. Kmvalues for glucose were 5.7 mM for the major fraction and 4.5 mM for the minor fraction. Neither fraction phosphorylated GlcNAc. A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Kmof 25 μ M for GlcNAc. Islet tissue also contained hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) eluting in multiple peaks. The results are consistent with the concept that glucokinase serves as the glucose sensor of pancreatic beta cells. |
| doi_str_mv | 10.1073/pnas.80.1.85 |
| format | Article |
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The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for both enzyme fraction. Kmvalues for glucose were 5.7 mM for the major fraction and 4.5 mM for the minor fraction. Neither fraction phosphorylated GlcNAc. A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Kmof 25 μ M for GlcNAc. Islet tissue also contained hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) eluting in multiple peaks. The results are consistent with the concept that glucokinase serves as the glucose sensor of pancreatic beta cells.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.80.1.85</identifier><identifier>PMID: 6337376</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Biochemistry ; Brain - enzymology ; Chromatography ; DNA ; Elution ; Enzymes ; glucokinase ; Glucokinase - isolation & purification ; Glucokinase - metabolism ; Hexokinase - metabolism ; Homogenization ; Islets of Langerhans ; Islets of Langerhans - enzymology ; Kinetics ; Liver ; Liver - enzymology ; Male ; Phosphorylation ; Rats</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1983-01, Vol.80 (1), p.85-89</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-cf4573a1fcf69cd39947f4174e6625b77d64c5f4dae70c90d06a32f1710260ee3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/80/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/13325$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/13325$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6337376$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meglasson, Martin D.</creatorcontrib><creatorcontrib>Burch, Pamela Trueheart</creatorcontrib><creatorcontrib>Berner, Donna K.</creatorcontrib><creatorcontrib>Najafi, Habiba</creatorcontrib><creatorcontrib>Vogin, Alan P.</creatorcontrib><creatorcontrib>Matschinsky, Franz M.</creatorcontrib><title>Chromatographic Resolution and Kinetic Characterization of Glucokinase from Islets of Langerhans</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) from rat islets of Langerhans was partially purified by chromatography on DEAE-Cibacron blue F3GA agarose. The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for both enzyme fraction. Kmvalues for glucose were 5.7 mM for the major fraction and 4.5 mM for the minor fraction. Neither fraction phosphorylated GlcNAc. A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Kmof 25 μ M for GlcNAc. Islet tissue also contained hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) eluting in multiple peaks. The results are consistent with the concept that glucokinase serves as the glucose sensor of pancreatic beta cells.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Brain - enzymology</subject><subject>Chromatography</subject><subject>DNA</subject><subject>Elution</subject><subject>Enzymes</subject><subject>glucokinase</subject><subject>Glucokinase - isolation & purification</subject><subject>Glucokinase - metabolism</subject><subject>Hexokinase - metabolism</subject><subject>Homogenization</subject><subject>Islets of Langerhans</subject><subject>Islets of Langerhans - enzymology</subject><subject>Kinetics</subject><subject>Liver</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>Phosphorylation</subject><subject>Rats</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>eNqFkc1v1DAUxC1EVZbCjRMIKQfEqVme46_kwAGtoK1YCQnB2biOvXHJ2lvbQcBfj9NdWjggTpb9m5n3rEHoCYYlBkFe7bxKy7Zcli27hxYYOlxz2sF9tABoRN3Shj5AD1O6AoCOtXCMjjkhggi-QF9WQwxblcMmqt3gdPXRpDBO2QVfKd9X7503uTyvBhWVzia6n-oGBludjZMOX10ZbypbUqqLNJqcZrRWfmPioHx6hI6sGpN5fDhP0Od3bz-tzuv1h7OL1Zt1rakQudaWMkEUttryTvek66iwFAtqOG_YpRA9p5pZ2isjQHfQA1eksVhgaDgYQ07Q633ubrrcml4bn6Ma5S66rYo_ZFBO_k28G-QmfJOkIwTT4n958MdwPZmU5dYlbcZReROmJFsgnFPg_xViwhgXfE483Qt1DClFY2-XwSDn5uTcXAmWWLasyJ__-YFb8aGqwp8d-Oz6Te_cL_5NpZ3GMZvvucie7mVXKYd4txAhDSO_AB7RtoY</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>Meglasson, Martin D.</creator><creator>Burch, Pamela Trueheart</creator><creator>Berner, Donna K.</creator><creator>Najafi, Habiba</creator><creator>Vogin, Alan P.</creator><creator>Matschinsky, Franz M.</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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19830101</creationdate><title>Chromatographic Resolution and Kinetic Characterization of Glucokinase from Islets of Langerhans</title><author>Meglasson, Martin D. ; Burch, Pamela Trueheart ; Berner, Donna K. ; Najafi, Habiba ; Vogin, Alan P. ; Matschinsky, Franz M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-cf4573a1fcf69cd39947f4174e6625b77d64c5f4dae70c90d06a32f1710260ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Brain - enzymology</topic><topic>Chromatography</topic><topic>DNA</topic><topic>Elution</topic><topic>Enzymes</topic><topic>glucokinase</topic><topic>Glucokinase - isolation & purification</topic><topic>Glucokinase - metabolism</topic><topic>Hexokinase - metabolism</topic><topic>Homogenization</topic><topic>Islets of Langerhans</topic><topic>Islets of Langerhans - enzymology</topic><topic>Kinetics</topic><topic>Liver</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>Phosphorylation</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meglasson, Martin D.</creatorcontrib><creatorcontrib>Burch, Pamela Trueheart</creatorcontrib><creatorcontrib>Berner, Donna K.</creatorcontrib><creatorcontrib>Najafi, Habiba</creatorcontrib><creatorcontrib>Vogin, Alan P.</creatorcontrib><creatorcontrib>Matschinsky, Franz M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</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>Meglasson, Martin D.</au><au>Burch, Pamela Trueheart</au><au>Berner, Donna K.</au><au>Najafi, Habiba</au><au>Vogin, Alan P.</au><au>Matschinsky, Franz M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chromatographic Resolution and Kinetic Characterization of Glucokinase from Islets of Langerhans</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>80</volume><issue>1</issue><spage>85</spage><epage>89</epage><pages>85-89</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) from rat islets of Langerhans was partially purified by chromatography on DEAE-Cibacron blue F3GA agarose. The enzyme eluted in two separate peaks. Sigmoidal rate dependence was found with respect to glucose (Hill coefficient = 1.5) for both enzyme fraction. Kmvalues for glucose were 5.7 mM for the major fraction and 4.5 mM for the minor fraction. Neither fraction phosphorylated GlcNAc. A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Kmof 25 μ M for GlcNAc. Islet tissue also contained hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) eluting in multiple peaks. The results are consistent with the concept that glucokinase serves as the glucose sensor of pancreatic beta cells.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6337376</pmid><doi>10.1073/pnas.80.1.85</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1983-01, Vol.80 (1), p.85-89 |
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| subjects | Animals Biochemistry Brain - enzymology Chromatography DNA Elution Enzymes glucokinase Glucokinase - isolation & purification Glucokinase - metabolism Hexokinase - metabolism Homogenization Islets of Langerhans Islets of Langerhans - enzymology Kinetics Liver Liver - enzymology Male Phosphorylation Rats |
| title | Chromatographic Resolution and Kinetic Characterization of Glucokinase from Islets of Langerhans |
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