Author: Maj M.C. Singh B. Gupta R.S.
Publisher: Elsevier
ISSN: 0006-291X
Source: Biochemical and Biophysical Research Communications, Vol.275, Iss.2, 2000-08, pp. : 386-393
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Abstract
The structure–activity relationship for Chinese hamster adenosine kinase (AK) was examined by making systematic deletions from the N- and C-terminal ends. The first 16 a.a. residues from the N-terminal end, which likely form a random coil, can be deleted without any effect on AK activity or stability. The successive removal of the next 11 residues, which stabilize the first β structure of the protein, leads to a progressive loss of AK activity from 100 to about 3%. The loss in activity is accompanied by increasing thermal instability and a slight increase in the
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