Chapter 1 advent (pages 1–4): G. V. R. Born
Chapter 2 universal Pathways of Membrane Reactivity after Stimulation of Platelets by way of various brokers (pages 5–21): Ernst F. Luscher and P. Massini
Chapter three Binding of Adenosine Diphosphate via Human Platelet Membrane (pages 23–46): Ralph L. Nachman
Chapter four Enzyme actions at the Platelet floor with regards to the motion of Adenosine Diphosphate (pages 47–75): J. Fraser Mustard, M. A. Packham, D. W. Perry, M. A. Guccione and R. L. Kinlough?Rathbone
Chapter five Stimulus?Response Coupling within the Thrombin?Platelet interplay (pages 77–100): Thomas C. Detwiler, Bernice M. Martin and Richard D. Feinman
Chapter 6 The interplay of Platelet Actin, Myosin and Myosin gentle Chain Kinase (pages 101–119): Robert S. Adelstein, Mary Anne Conti, James L. Daniel and William Anderson
Chapter 7 Roles of Cyclic Nucleotides in Platelet functionality (pages 121–151): Richard J. Haslam
Chapter eight preliminary Biochemical Responses of Platelets to Stimulation (pages 153–173): D. C. B. Mills
Chapter nine Biochemistry of the Platelet unlock response (pages 175–205): Holm Holmsen
Chapter 10 Prostaglandins and Precursors in Platelet functionality (pages 207–224): J. Bryan Smith, Carol M. Ingerman and Melvin J. Silver
Chapter eleven value of Glucose and Glycogen Metabolism for Platelet functionality (pages 225–238): W. Schneider and A. R. L. Gear
Chapter 12 Elemental Composition of Platelet Dense our bodies (pages 239–259): R. J. Skaer
Chapter thirteen The Organelles Storing 5?Hydroxytryptamine in Blood Platelets (pages 261–286): A. Pletscher and M. Da Prada
Chapter 14 5?Hydroxytryptamine Receptors of Platelets (pages 287–307): G. V. R. Born and F. Michal
Chapter 15 Interactions among 5?Hydroxytryptamine and Platelet Lipid Fractions (pages 309–342): Aaron J. Marcus, Lenore B. Safier and Harris L. Ullman
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Additional info for Ciba Foundation Symposium 35 - Biochemistry and Pharmacology of Platelets
This caused markedly enhanced conversion of [14C]ADP to [14C]ATP and of [14C]GDP to [14C]GTP, but only slightly enhanced the conversion of [14C]CDP to [l4C]CTP. The effect of nucleoside mono-, di- and triphosphates on rabbit platelets is summarized in Table 2. Results of experiments on the aggregation of platelets are also included. With the exception of AMP, the nucleoside monophosphates had little effect on ADP-induced platelet aggregation or on the conversion of [14C]ADP to [14C]ATP. At the concentrations tested, only AMP 52 J.
Left: Coomassie blue stained gel for proteins. Right: PAS stain for glycoproteins. Anode at the bottom. membrane vesicles in an aqueous buffer system with ['4C]ADP. The binding of labelled ADP to platelet membranes was measured by three methods (Nachman & Ferris 1974). In the centrifugation method, [I4C]ADP was incubated with a membrane suspension (200 to 300 pg) in a 1 ml volume for 60 minutes at 37 "C with shaking. The suspension was diluted with buffer and ultracentrifuged. The membrane pellet was resuspended in buffer, washed twice and then measured for the amount of retained radioactivity.
Dephosphorylation of the bound ATP occurs during polymerization. In both forms of actin the nucleotide is not apparently covalently linked and is to some extent exchangeable (Laki 1971). In our subcellular fractionation studies we use zonal rotor ultracentrifugation and we have one procedure for isolating the membrane and granular organelles (lysosome-likegranules, mitochondria, 5-hydroxytryptamine storage bodies) in one single gradient run (Taylor & Crawford 1974a) and another which separates the mixed membrane fraction into surface and intracellular membrane vesicles (Taylor & Crawford 19743).
Ciba Foundation Symposium 35 - Biochemistry and Pharmacology of Platelets