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Cloning and characterization of cDNA for human adenylate kinase 2A

Authors
Lee, YKim, JWLee, IAKang, HBChoe, YKLee, HGLim, JSKim, HJPark, CChoe, IS
Issue Date
Jul-1996
Publisher
Academic Press
Citation
Biochemistry and Molecular Biology International, v.39, no.4, pp 833 - 842
Pages
10
Journal Title
Biochemistry and Molecular Biology International
Volume
39
Number
4
Start Page
833
End Page
842
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/150766
DOI
10.1080/15216549600201931
ISSN
1039-9712
Abstract
We have isolated and characterized a cDNA clone encoding human adenylate kinase 2A (AK2A) from cDNA libraries of fetal liver origin. The complete nucleotide sequence of the cloned 889 nucleotide cDNA fragment indicated that the deduced gene product of human AK2A is composed of 239 amino acids with a molecular weight of 26 kD. Comparison of these nucleotide and amino acid sequences with the corresponding sequences of bovine AK2A and rat AK2 revealed a high degree of conservation. It showed 91% and 98% homologies in DNA and amino acid sequences, respectively, with bovine AK2A throughout the full open reading frame. RNA blot analysis revealed that three species of mRNA were present with approximate 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.
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