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Isoenzymes of GMP Kinase From L1210 Cells: Isolation and Characterization

机译:L1210细胞中GMP激酶的同工酶:分离与鉴定

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摘要

Guanylate Kinase from a mouse leukemic L1210 cells has been purified nearly to homogeneity for the first time. It consists of five isoenzymes with pI 5.95, 5.50, 5.08, 4.83 and 4.51, respectively. The native enzyme is a monomer with a relative molecular mass 25 000. The kinetic constants K_m' V_(max) and K_(cat)/K_m of isoenzymes were estimated. The purified GMP kinase is absolutely specific to GMP and/or dGMP as phosphate acceptor but has a broad specificity to nucleoside 5'-triphosphates as phosphate donors.
机译:来自小鼠白血病L1210细胞的鸟苷酸激酶首次被纯化至近乎同质。它由五个pI分别为5.95、5.50、5.08、4.83和4.51的同工酶组成。天然酶是相对分子质量为25 000的单体。估计了同工酶的动力学常数K_m'V_(max)和K_(cat)/ K_m。纯化的GMP激酶对作为磷酸盐受体的GMP和/或dGMP具有绝对的特异性,但对作为磷酸盐供体的5'-三磷酸核苷具有广泛的特异性。

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