在37摄氏度和4摄氏度下，固定化凝血酶刺激血小板中的蛋白质磷酸化。 - Suppr | 超能文献

Protein phosphorylation in platelets stimulated by immobilized thrombin at 37 degrees and 4 degrees C.

作者信息

Wallace W C, Bensusan H B

出版信息

J Biol Chem. 1980 Mar 10;255(5):1932-7.

Abstract

摘要

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Protein phosphorylation in platelets stimulated by immobilized thrombin at 37 degrees and 4 degrees C.在37摄氏度和4摄氏度下，固定化凝血酶刺激血小板中的蛋白质磷酸化。

J Biol Chem. 1980 Mar 10;255(5):1932-7.

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Inhibitory action of guanosine 3', 5'-monophosphate on thrombin-induced phosphatidylinositol turnover and protein phosphorylation in human platelets.3',5'-环磷酸鸟苷对凝血酶诱导的人血小板磷脂酰肌醇代谢及蛋白质磷酸化的抑制作用

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3

The action of the protein kinase C inhibitor, staurosporine, on human platelets. Evidence against a regulatory role for protein kinase C in the formation of inositol trisphosphate by thrombin.蛋白激酶C抑制剂星形孢菌素对人血小板的作用。关于蛋白激酶C在凝血酶诱导肌醇三磷酸形成中起调节作用的证据不足。

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4

Determination of basal and stimulated levels of inositol triphosphate in [32P]orthophosphate-labeled platelets.

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5

Characterization of a platelet protein phosphorylated during the thrombin-induced release reaction.凝血酶诱导释放反应过程中磷酸化的血小板蛋白的特性分析。

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6

Sodium fluoride prevents receptor- and protein kinase C-mediated activation of the human platelet Na+/H+ exchanger without inhibiting its basic pHi-regulating activity.氟化钠可防止受体和蛋白激酶C介导的人血小板钠/氢交换体的激活，而不抑制其调节细胞内pH值的基本活性。

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7

The effects of platelet secretion inhibitors on protein phosphorylation.血小板分泌抑制剂对蛋白质磷酸化的影响。

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8

Phosphorylation of platelet microtubule proteins by an endogenous protein kinase.

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9

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10

Effect of chlorpromazine on inositol-lipid signalling system in human thrombocytes.氯丙嗪对人血小板中肌醇-脂质信号系统的影响。

Physiol Bohemoslov. 1987;36(6):495-501.

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Biochem J. 2000 Jan 15;345 Pt 2(Pt 2):307-14.

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Phosphorylation of parathyroid secretory protein.甲状旁腺分泌蛋白的磷酸化

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3

Potentiation by thrombin of the secretion of serotonin from permeabilized platelets equilibrated with Ca2+ buffers. Relationship to protein phosphorylation and diacylglycerol formation.凝血酶对用Ca2+缓冲液平衡的透化血小板中5-羟色胺分泌的增强作用。与蛋白质磷酸化和二酰基甘油形成的关系。

Biochem J. 1984 Sep 1;222(2):351-61. doi: 10.1042/bj2220351.