Y. Lee et al., CLONING AND CHARACTERIZATION OF CDNA FOR HUMAN ADENYLATE KINASE 2A, Biochemistry and molecular biology international, 39(4), 1996, pp. 833-842
We have isolated and characterized a cDNA clone encoding human adenyla
te kinase 2A (AK2A) from cDNA libraries of fetal liver origin. The com
plete nucleotide sequence of the cloned 889 nucleotide cDNA fragment i
ndicated that the deduced gene product of human AK2A is composed of 23
9 amino acids with a molecular weight of 26 kD. Comparison of these nu
cleotide and amino acid sequences with the corresponding sequences of
bovine AK2A and rat AK2 revealed a high degree of conservation. It sho
wed 91% and 98% homologies in DNA and amino acid sequences, respective
ly, with bovine AK2A throughout the full open reading frame. RNA blot
analysis revealed that three species of mRNA were present with approxi
mate sizes of 3.4, 2.1, and 1.0 kb. This gene was expressed in E. coli
cells and the recombinant protein was enzymatically active.