在HL-60早幼粒细胞白血病细胞核提取物中鉴定出一种针对磷酸肽焦谷氨酸-天冬氨酸-天冬氨酸-丝氨酸（磷酸化）-天冬氨酸-谷氨酸-谷氨酸-天冬酰胺的磷酸酶活性。
Identification of a phosphatase activity, toward the phosphopeptide pyroGlu-Asp-Asp-Ser(p)-Asp-Glu-Glu-Asn, in nuclear extract from HL-60 promyelocitic leukaemia cells.
作者信息
Cardellini E, Nardicchi V, Macchioni L
机构信息
Dipartimento di Biologia Cellulare e Molecolare, Sezione di Fisiologia e Biofisica, Università di Perugia, Via Pascoli, 1-06123 Perugia, Italy.
出版信息
Physiol Chem Phys Med NMR. 2000;32(1):27-33.
PMID:10970045
Abstract
Total protein extract from HL-60 cells was found to be able to dephosphorylate the RNA polymerase II octapeptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn previously phosphorylated with protein kinase CKII (pCKII). Fractionation in cytoplasm, nuclear and chromatin extracts shows the phosphatase activity to be localized only in the nucleus, but not to be bound to the chromatin.
摘要
研究发现，HL-60细胞的总蛋白提取物能够使先前被蛋白激酶CKII（pCKII）磷酸化的RNA聚合酶II八肽焦谷氨酸-天冬氨酸-天冬氨酸-丝氨酸-天冬氨酸-谷氨酸-谷氨酸-天冬酰胺去磷酸化。对细胞质、细胞核和染色质提取物进行分级分离显示，磷酸酶活性仅定位于细胞核，而不与染色质结合。
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