Chan P K, Liu Q R, Durban E
Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030.
Biochem J. 1990 Sep 1;270(2):549-52. doi: 10.1042/bj2700549.
Nucleophosmin (B23) was phosphorylated in vitro with [gamma-32P]ATP and a nuclear kinase (type II) purified from HeLa cells. The phosphorylation was inhibited by heparin and by 2,3-diphosphoglycerate. Peptide mapping analysis indicated that the phosphorylation site in vitro was identical to that in vivo. Purified nucleoli have a similar kinase that phosphorylated nucleophosmin at the same site. These results indicated that nucleophosmin is phosphorylated in vivo by a nucleolar kinase (type II).
用[γ-32P]ATP和从HeLa细胞中纯化的一种核激酶（II型）在体外对核磷蛋白（B23）进行磷酸化。肝素和2,3-二磷酸甘油酸可抑制这种磷酸化。肽图谱分析表明，体外的磷酸化位点与体内的相同。纯化的核仁具有一种类似的激酶，可在相同位点使核磷蛋白磷酸化。这些结果表明，核磷蛋白在体内被一种核仁激酶（II型）磷酸化。
