Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase
Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of fi...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1974-04, Vol.71 (4), p.1384-1387 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 71 |
| creator | S. A. G. J. Witteveen Sobel, B. E. DeLuca, M. |
| description | Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the isoenzyme pattern of the serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively. |
| doi_str_mv | 10.1073/pnas.71.4.1384 |
| format | Article |
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The MB isoenzyme appearing in this condition could be detected quantitatively.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.71.4.1384</identifier><identifier>PMID: 4524644</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenosine Triphosphate - biosynthesis ; Biological Sciences: Medical Sciences ; Bioluminescence ; Creatine ; Creatine Kinase - blood ; Creatine Kinase - metabolism ; Diagnosis, Differential ; Electrophoresis ; Enzymes ; Humans ; Insecta ; Isoenzymes - blood ; Isoenzymes - metabolism ; Kinetics ; Light emission ; Luciferases ; Luminescent Measurements ; Muscle tissues ; Myocardial infarction ; Myocardial Infarction - blood ; Myocardial Infarction - diagnosis ; Myocardial Infarction - metabolism ; Phosphates ; Skeletal muscle</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1974-04, Vol.71 (4), p.1384-1387</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3714-38fcf5feed5db08b8d937829067df266efb5bd15a7f703e0df2574d4bc0834bc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/71/4.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/63333$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/63333$$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/4524644$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>S. A. G. J. Witteveen</creatorcontrib><creatorcontrib>Sobel, B. E.</creatorcontrib><creatorcontrib>DeLuca, M.</creatorcontrib><title>Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the isoenzyme pattern of the serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively.</description><subject>Adenosine Triphosphate - biosynthesis</subject><subject>Biological Sciences: Medical Sciences</subject><subject>Bioluminescence</subject><subject>Creatine</subject><subject>Creatine Kinase - blood</subject><subject>Creatine Kinase - metabolism</subject><subject>Diagnosis, Differential</subject><subject>Electrophoresis</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Insecta</subject><subject>Isoenzymes - blood</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Light emission</subject><subject>Luciferases</subject><subject>Luminescent Measurements</subject><subject>Muscle tissues</subject><subject>Myocardial infarction</subject><subject>Myocardial Infarction - blood</subject><subject>Myocardial Infarction - diagnosis</subject><subject>Myocardial Infarction - metabolism</subject><subject>Phosphates</subject><subject>Skeletal muscle</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kL9v1DAYhi0EKtfC2gEJKVO3hM-xEzsDA7rSH6ISHWC2nORzLyWJg-1Ubf96HN31dF3wYEvf-zy29RJySiGjINiXadQ-EzTjGWWSvyErChVNS17BW7ICyEUqec7fk2Pv7wGgKiQckSNe5LzkfEXOf3Qjhq5Jbp2d0IUOfWJNEjaYXHuL4_PTsJ1czYMek7VDHaKR3G6snzb2Txefxw_kndG9x4-784T8vvj-a32V3vy8vF5_u0kbJihPmTSNKQxiW7Q1yFq2FRMyr6AUrcnLEk1d1C0ttDACGEIcFoK3vG5AsrizE_J1e-801wO2DY7B6V5Nrhu0e1JWd-p1MnYbdWcfFJMyZyz6Zzvf2b8z-qCGzjfY93pEO3sVoVIIKCKYbcHGWe8dmv0bFNRSu1pqV4Iqrpbao_D58Gd7fNfzQb54L-mhf_a_XJm57wM-hgh-2oL3Pli3J0u2rH9dLKCe</recordid><startdate>19740401</startdate><enddate>19740401</enddate><creator>S. A. G. J. Witteveen</creator><creator>Sobel, B. E.</creator><creator>DeLuca, 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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19740401</creationdate><title>Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase</title><author>S. A. G. J. Witteveen ; Sobel, B. 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A. G. J. Witteveen</creatorcontrib><creatorcontrib>Sobel, B. E.</creatorcontrib><creatorcontrib>DeLuca, 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>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>S. A. G. J. Witteveen</au><au>Sobel, B. 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With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the isoenzyme pattern of the serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4524644</pmid><doi>10.1073/pnas.71.4.1384</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1974-04, Vol.71 (4), p.1384-1387 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_71_4_1384 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphate - biosynthesis Biological Sciences: Medical Sciences Bioluminescence Creatine Creatine Kinase - blood Creatine Kinase - metabolism Diagnosis, Differential Electrophoresis Enzymes Humans Insecta Isoenzymes - blood Isoenzymes - metabolism Kinetics Light emission Luciferases Luminescent Measurements Muscle tissues Myocardial infarction Myocardial Infarction - blood Myocardial Infarction - diagnosis Myocardial Infarction - metabolism Phosphates Skeletal muscle |
| title | Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase |
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