Chang L M, Bollum F J
J Biol Chem. 1982 Aug 25;257(16):9588-92.
Incubation of human lymphoblastoid cell extracts in the presence of cAMP and ATP produces changes in the chromatographic pattern of terminal transferase activity separated on phosphocellulose columns. Incubation of high molecular weight and low molecular weight preparations of calf thymus terminal transferase with the catalytic subunit of beef cardiac muscle cAMP-dependent protein kinase and [gamma-32P]ATP result in phosphorylation of the 58,000-dalton form of the enzyme and no other lower molecular weight terminal peptides. These results, taken with our earlier results on tissue proteolysis of terminal transferase to lower molecular weight, active forms (Chang, L. M. S., Plevani, P., and Bollum, F. J. (1982) J. Biol. Chem. 257, 5700-5706), resolve the heterogeneity observed with various preparations of the enzyme.
在环磷酸腺苷（cAMP）和三磷酸腺苷（ATP）存在的情况下，对人淋巴母细胞提取物进行温育，会使在磷酸纤维素柱上分离的末端转移酶活性的色谱图谱发生变化。用牛肉心肌cAMP依赖性蛋白激酶的催化亚基和[γ-32P]ATP对小牛胸腺末端转移酶的高分子量和低分子量制剂进行温育，会导致该酶58,000道尔顿形式的磷酸化，而没有其他更低分子量的末端肽。这些结果，结合我们早期关于末端转移酶组织蛋白水解为更低分子量活性形式的结果（张，L.M.S.，普莱瓦尼，P.，和博勒姆，F.J.（1982年）《生物化学杂志》257，5700 - 5706），解决了在该酶的各种制剂中观察到的异质性问题。
