Isolation and Immunological Properties of Adenosine Kinase

Abstract

Bovine liver adenosine kinase is a 43 kDa protein that catalyzes the transfer of phosphate from GTP or ATP to adenosine. Its immunological properties were compared to other GTP-binding proteins of approximately 40 kDa, in particular those involved in signal transduction, such as Gs and Gi, the stimulatory and inhibitory regulatory proteins of adenylyl cyclase, Gt, from the visual excitation system, and Go, a similar protein of unknown function. Antibodies elicited in rabbits against adenosine kinase did not significantly cross-react with other guanyl nucleotide-binding proteins. Antibodies against the other GTP-binding proteins did not react with adenosine kinase. Thus these GTP-binding proteins do not exhibit immunological cross-reactivity.

Intrinsic tryptophan fluorescence of bovine liver adenosine kinase, characterization of ligand binding sites and conformational changes

“…Bovine liver adenosine kinase is monomeric with an apparent molecular mass of about 45 kDa. This value is well correlated with the previous determination of the enzyme molecular mass of 43 kDa (Noda et al, 1989) aind with the molecular mass of other adenosine kinases (Andres and Fox 1979;Rotllan and Miras Plortugal. 1985).…”

“…An apparent K,,, value of 0.26 mM was determined for ATP, which is of the same order as the K,, values for other adenosine kinases (betwen 0.02 and 0.6 mM) (Palella et al, 1980;Yamada et al, 1980). In contrast, it is markedly ttifferent from the K,, value of 8 pM determined previously for the same enzyme (Noda et al, 1989).…”

“…In contrast, it is markedly ttifferent from the K,, value of 8 pM determined previously for the same enzyme (Noda et al, 1989).…”