By Chi-Ying F. Huang, Chiun-Jye Yuan, Nataliya B. Livanova, Donald J. Graves (auth.), R. L. Khandelwal, J. H. Wang (eds.)
This ebook, released in organization with the magazine MOLECULAR ANDCELLULAR BIOCHEMISTRY, is devoted to Ed Krebs and Eddy Fischer in occasion in their 1992 Nobel Prize in body structure and drugs. Reversible protein phosphorylation is a study box pioneered and built through Krebs and Fischer. This booklet includes brief reports and unique study papers contributed by means of Krebs and Fischer's coworkers, either former and present.
The contents mirror the two-way interplay among protein phosphorylation and different biomedical examine fields. The chapters are grouped into 4 sections. the 1st take care of structure/function elements of protein kinases and protein mechanisms. not like many different study fields, which endure classes of excessive job and productiveness by means of relative calm, the protein phosphorylation box loved persisted development either in scope and depth, and the velocity of this progress has elevated markedly lately. This quantity will offer a glimpse of the dynamism and variety of the learn task consultant of the present country of the sector.
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Extra resources for Reversible Protein Phosphorylation in Cell Regulation
21]. Catalytic assays Phosphorylase kinase was assayed initially by monitor- 33 ing the concentration of phosphorylase a in the original two-step incubation procedure . We subsequently devised a continuous fluorometric assay based on differences in the binding of 1-anilinonaphthalene-8-sulfonate (ANS) by phosphorylase b and a . 0ml (lOmm cuvette). lmM CaCI2 ; for experiments done in the absence of calcium, the solution contained 1mM EGTA. Fluorescence changes were monitored continuously with the Perkin Elmer LS-50 fluorometer (interfaced with a 386 IBM compatible computer), employing excitation and emission wavelengths of 360nm and 460nm.
0mM Mg++ versus 12mM) and temperature 23°-26° vs 30°) used in the assays [22, 23], these specific activities are lower than some of the values previously reported for phosphorylase kinase. or that (4) Identification of phosphorylation sites in the 33 kD catalytically active fragment The plots in Fig. tm/min. Clearly, the results of the two methods are similar - with small differences that are within the range of error. Applications of the fluorometric assay appear in Fig. 2 The side by side Coomassie blue-stained electrophoresis gel and autoradiograph in Fig.
Haschke RH, Fischer EH: Control of phosphorylase activity in a muscle glycogen particle. 1970 Heilmeyer LMG lr. Groschel-Stewart U. lahnke U. Kilimann MW, Kohse KP. Varsanyi M: Novel aspects of skeletal muscle protein kinase and protein phosphatase regulation by Ca 2 +. ): Cellular regulation by protein phosphorylation. Springer-Verlag. Berlin. Heidelberg. New York. London. Paris, Tokyo. Hong Kong. Barcelona. Budapest. 1991 Heilmeyer LMG lr: Molecular basis of signal integration in phosphorylase kinase.
Reversible Protein Phosphorylation in Cell Regulation by Chi-Ying F. Huang, Chiun-Jye Yuan, Nataliya B. Livanova, Donald J. Graves (auth.), R. L. Khandelwal, J. H. Wang (eds.)