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J. Biochem, 1996, Vol. 119, No. 4 719-724
© 1996 Japanese Biochemical Society

research-article

N{omega}-Phosphoarginine Phosphatase (17 kDa) and Alkaline Phosphatase as Protein Arginine Phosphatases1

Akira Kumon*, Hiroaki Kodama{dagger}, Michio Kondo{dagger}, Fumiaki Yokoi* and Hiroyuki Hiraishi*

*Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849
{dagger}Department of Chemistry, Faculty of Science and Engineering, Saga University Honjyo 1, Saga, Saga 840

Seven synthetic polymers,(Glu4,Tyr)n, (Arg)n, (Arg, Pro, Thr)n (Arg-Gly-Glu)6, (Arg-Gly-Phe)5, (Glu-Arg-Gly-Phe)5, and (Ala-Leu-Arg-Arg-Ile-Arg-Gly-Glu-Arg)2, were treated with phosphoryl chloride to phosphorylate their Tyr, Thr, and Arg residues. Protamines and histories were phosphorylated similarly. These phosphorylated peptides were examined as to whether or not they serve as substrates for intestinal alkaline phosphatase [EC 3.1.3.1 [EC] ] and liver N{omega}-phosphoarginine phosphatase [Kuba, M., Ohmori, H., and Kumon, A. (1992)Eur. J. Biochenu 208, 747-752]. Phosphorylated polyarginine was hydrolyzed with a lower Km with alkaline phosphatase than with N{omega}-phosphoarginine phosphatase, while the phosphorylated forms of (Arg-Gly-Phe)6 and culpeine were better substrates for N{omega}-phosphoarginine phosphatase. When (Arg, Pro, Thr)n and culpeine were phosphorylated chemically after treatment with phenylglyoxal, these phosphorylated peptides were worse substrates for N{omega}-phosphoarginine phosphatase than for alkaline phosphatase. Moreover, the results of proton-decoupled 31P NMR analysis indicated that N{omega}-phosphoar-ginine phosphatase released P1 from N{omega}-phosphoarginine residues of phosphopeptides. These results indicate that both phosphatases function as protein arginine phosphatases in different manners, and thatN{omega}-phosphoarginine phosphatase is useful for selectively detecting N{omega}-phosphoarginine residue in peptides containing various kinds of phosphorylated amino acids.

1This work was supported in part by Granta-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan.


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