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在肝素存在的情况下,CKI和CKII对酵母核糖体蛋白的磷酸化作用。

Phosphorylation of yeast ribosomal proteins by CKI and CKII in the presence of heparin.

作者信息

Wojda I, Cytryńska M, Frajnt M, Jakubowicz T

机构信息

Department of Molecular Biology, Institute of Microbiology and Biotechnology, Maria Curie-Skłodowska University, Lublin, Poland.

出版信息

Acta Biochim Pol. 1999;46(1):211-5.

Abstract

We have found that heparin has a different effect on Trichosporon cutaneum ribosomal protein phosphorylation by CKI and by CKII. In the presence of heparin, modification of 13 kDa, 19 kDa and 38 kDa proteins catalyzed by CKII was inhibited, while in the case of CKI, in addition to protein of 15 kDa, phosphorylation of 20 kDa and 35 kDa proteins was detected. It was also found that, in the presence of heparin, phosphorylation of P proteins (13 kDa and 38 kDa) by ribosome-bound protein kinases was inhibited. Moreover at the same conditions modification of 40 kDa protein was observed in all four yeast species tested.

摘要

我们发现,肝素对皮状丝孢酵母核糖体蛋白由酪蛋白激酶I(CKI)和酪蛋白激酶II(CKII)催化的磷酸化作用具有不同影响。在肝素存在的情况下,CKII催化的13 kDa、19 kDa和38 kDa蛋白的修饰受到抑制,而对于CKI,除了15 kDa蛋白外,还检测到20 kDa和35 kDa蛋白的磷酸化。还发现,在肝素存在的情况下,核糖体结合蛋白激酶对P蛋白(13 kDa和38 kDa)的磷酸化受到抑制。此外,在相同条件下,在所测试的所有四种酵母菌种中均观察到40 kDa蛋白的修饰。

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