Takio K, Kuenzel E A, Walsh K A, Krebs E G
Proc Natl Acad Sci U S A. 1987 Jul;84(14):4851-5. doi: 10.1073/pnas.84.14.4851.
The amino acid sequence of the 209-residue beta subunit of bovine lung casein kinase II has been determined. Excluding the amino-terminal blocking group, which was not identified, the molecular weight of the polypeptide chain is 24,239. A marked polarity of the beta subunit is indicated by clusters of negative charges in the amino-terminal region and of positive charges in the carboxyl-terminal region. Whereas the beta subunit shows no homology with any known protein, a segment of the sequence of the larger and microheterogeneous alpha subunit exhibits homology with the catalytic domains of other protein kinases, particularly with the yeast cell-division-control protein CDC28.
已确定牛肺酪蛋白激酶II 209个残基的β亚基的氨基酸序列。除未确定的氨基末端封闭基团外,多肽链的分子量为24239。β亚基的显著极性表现为氨基末端区域的负电荷簇和羧基末端区域的正电荷簇。虽然β亚基与任何已知蛋白质均无同源性,但较大且微不均一的α亚基的一段序列与其他蛋白激酶的催化结构域具有同源性,特别是与酵母细胞分裂控制蛋白CDC28。