An automated assay for phosphorylase kinase
Identifieur interne : 005059 ( Istex/Corpus ); précédent : 005058; suivant : 005060An automated assay for phosphorylase kinase
Auteurs : H. P. Jennissen ; L. M. G. Heilmeyer Jr.Source :
- Analytical Biochemistry [ 0003-2697 ] ; 1973.
Abstract
A fully automated assay of phosphorylase kinase capable of processing 40 samples/hr is described. Problems due to enzyme adsorbed to the incubation coil and thereby producing a continuous rise of the base line were overcome by washing with a solution containing 0.05% Triton X-100, 0.03% SDS, and 5 mm EDTA. Under these conditions, a linear relationship between phosphorylase kinase concentration in the incubation mixture and absorbancy at pH's 6.8 and 8.2 is obtained when 1% glycogen is present in the reaction mixture.Inclusion of glycogen allows reduction of the concentration of phosphorylase in the incubation mixture. Due to the presence of Triton X-100 in this test, the carbohydrate acts like an allosteric activator of phosphorylase kinase. The standard deviation of the automated kinase test is 1.3% lower than that of the manual test.
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DOI: 10.1016/0003-2697(74)90058-X
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Problems due to enzyme adsorbed to the incubation coil and thereby producing a continuous rise of the base line were overcome by washing with a solution containing 0.05% Triton X-100, 0.03% SDS, and 5 mm EDTA. Under these conditions, a linear relationship between phosphorylase kinase concentration in the incubation mixture and absorbancy at pH's 6.8 and 8.2 is obtained when 1% glycogen is present in the reaction mixture.Inclusion of glycogen allows reduction of the concentration of phosphorylase in the incubation mixture. Due to the presence of Triton X-100 in this test, the carbohydrate acts like an allosteric activator of phosphorylase kinase. The standard deviation of the automated kinase test is 1.3% lower than that of the manual test.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>H.P. 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Under these conditions, a linear relationship between phosphorylase kinase concentration in the incubation mixture and absorbancy at pH's 6.8 and 8.2 is obtained when 1% glycogen is present in the reaction mixture.Inclusion of glycogen allows reduction of the concentration of phosphorylase in the incubation mixture. Due to the presence of Triton X-100 in this test, the carbohydrate acts like an allosteric activator of phosphorylase kinase. 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Problems due to enzyme adsorbed to the incubation coil and thereby producing a continuous rise of the base line were overcome by washing with a solution containing 0.05% Triton X-100, 0.03% SDS, and 5 mm EDTA. Under these conditions, a linear relationship between phosphorylase kinase concentration in the incubation mixture and absorbancy at pH's 6.8 and 8.2 is obtained when 1% glycogen is present in the reaction mixture.Inclusion of glycogen allows reduction of the concentration of phosphorylase in the incubation mixture. Due to the presence of Triton X-100 in this test, the carbohydrate acts like an allosteric activator of phosphorylase kinase. 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Problems due to enzyme adsorbed to the incubation coil and thereby producing a continuous rise of the base line were overcome by washing with a solution containing 0.05% Triton X-100, 0.03% SDS, and 5 m<ce:small-caps>m</ce:small-caps> EDTA. Under these conditions, a linear relationship between phosphorylase kinase concentration in the incubation mixture and absorbancy at pH's 6.8 and 8.2 is obtained when 1% glycogen is present in the reaction mixture.</ce:simple-para><ce:simple-para view="all" id="simple-para.0015">Inclusion of glycogen allows reduction of the concentration of phosphorylase in the incubation mixture. Due to the presence of Triton X-100 in this test, the carbohydrate acts like an allosteric activator of phosphorylase kinase. 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Ii. A.. %IIWER. W. I,., ASU FISCI~L':R. E. H.</editor><imprint><date type="published" when="1022"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">I</forename><surname>Hkilmeter</surname></persName></author><author><persName><forename type="first">/</forename></persName></author><author><persName><forename type="first">I</forename><forename type="middle">G</forename><surname>Jil</surname></persName></author><author><persName><forename type="middle">F</forename><surname>Mixiw</surname></persName></author><author><persName><forename type="middle">R H</forename><surname>Hascx~</surname></persName></author><author><persName><forename type="first">E</forename><forename type="middle">H</forename><surname>And</surname></persName></author></analytic><monogr><title level="j">J. Biol. Chern</title><imprint><biblScope unit="volume">245</biblScope><biblScope unit="page">6649</biblScope><date type="published" when="1970"></date></imprint></monogr></biblStruct><biblStruct><analytic></analytic><monogr><title level="j">J. Hiol. Chern</title><editor>I~ROSTROM. C. 0.. HUNKIELER. F</editor><editor>. I,.. ASI) KREBS. I?. (</editor><editor>.</editor><imprint><biblScope unit="volume">246</biblScope><date type="published" when="1961"></date></imprint></monogr></biblStruct><biblStruct><analytic></analytic><monogr><title level="j">J. Hiol. Chem</title><editor>W.41.511. D. A.. PERKISS. J. P.. BRO~TROM, (1. 0.. Ho, E</editor><editor>. S.. 4%~ KREHS. E. C,.</editor><imprint><biblScope unit="volume">246</biblScope><date type="published" when="1971"></date></imprint></monogr></biblStruct><biblStruct><monogr><editor>POWER. .J. u., H.412I_\1ERnLliIYTRR. k-. F,.. ~~R.4'LWI,D. (</editor><editor>. E., ASD k-REHS</editor></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">E</forename></persName></author></analytic><monogr><title level="j">Biochemistry</title><imprint><biblScope unit="volume">3</biblScope><date type="published" when="1040"></date></imprint></monogr></biblStruct><biblStruct><analytic></analytic><monogr><title level="m">237, 1244. S. FISKE. C. H.. .4s1) SLBBAROTV</title><editor>RL-,T(.HI.:R. R. FT.'.. ASU SI.TIIERI,.INIJ. E:. W'</editor><editor>.</editor><imprint><date type="published" when="1925"></date><biblScope unit="page">375</biblScope></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">Hawhke</forename><forename type="middle">R H</forename><surname>Asd H~</surname></persName></author></analytic><monogr><title level="j">Awl. Biochem</title><editor>II.M~TI:R. I,. hf. G., JR.</editor><imprint><biblScope unit="volume">47</biblScope><biblScope unit="page">451</biblScope><date type="published" when="1972"></date></imprint></monogr></biblStruct><biblStruct><monogr><author><persName><forename type="first">E</forename><surname>Hel~~icii</surname></persName></author><author><persName><surname>Mich</surname></persName></author><author><persName><surname>Aei</surname></persName></author><author><persName><forename type="first">M. C..</forename><surname>Ides</surname></persName></author><author><persName><forename type="middle">C F</forename><surname>\sd &ri</surname></persName></author><imprint><date type="published" when="1967"></date><biblScope unit="page">3695</biblScope></imprint></monogr><note>Biochcv~~i. .rtq 6</note></biblStruct><biblStruct><analytic><author><persName><forename type="first">P</forename><surname>Cohen</surname></persName></author></analytic><monogr><title level="j">Eur. J. Biochem</title><imprint><biblScope unit="volume">34</biblScope><biblScope unit="issue">1</biblScope><date type="published" when="1973"></date></imprint></monogr></biblStruct><biblStruct><monogr><author><persName><forename type="first">H</forename><forename type="middle">P</forename><surname>Jiwxissen</surname></persName></author><author><persName><forename type="first">.</forename><forename type="middle">W H</forename><surname>H~ri</surname></persName></author><author><persName><forename type="first">.</forename><forename type="middle">I M</forename><surname>And Hiulxie~er</surname></persName></author><author><persName><forename type="middle">.</forename><surname>Ct</surname></persName></author><author><persName><surname>Jr</surname></persName></author><imprint><date type="published" when="1973"></date></imprint></monogr></biblStruct><biblStruct><analytic></analytic><monogr><title level="j">Physiol. Chem</title><imprint><biblScope unit="volume">354</biblScope><biblScope unit="page">236</biblScope></imprint></monogr></biblStruct><biblStruct><monogr><author><persName><forename type="first">T</forename><surname>Hayakawa</surname></persName></author><author><persName><forename type="middle">J P</forename><surname>Perkiss</surname></persName></author><author><persName><forename type="middle">E G</forename><surname>And Krebs</surname></persName></author><imprint><date type="published" when="1973"></date><biblScope unit="page">574</biblScope></imprint></monogr><note>Biochemi. .sfr,q 12</note></biblStruct></listBibl></back></text></istex:refBibTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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