caa a22 4500 397557574 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021301 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021301 Nω-Phosphoarginine Phosphatase (17 kDa) and Alkaline Phosphatase as Protein Arginine Phosphatases [Elektronische Daten] [Akira Kumon, Hiroaki Kodama, Michio Kondo, Fumiaki Yokoi, Hiroyuki Hiraishi] 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] and liver Nω-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 Nω-phosphoarginine phosphatase, while the phosphorylated forms of (Arg-Gly-Phe)6 and culpeine were better substrates for Nω-phosphoarginine phosphatase. When (Arg, Pro, Thr)n and culpeine were phosphorylated chemically after treatment with phenylglyoxal, these phosphorylated peptides were worse substrates for Nω-phosphoarginine phosphatase than for alkaline phosphatase. Moreover, the results of proton-decoupled 31P NMR analysis indicated that Nω-phosphoar-ginine phosphatase released P1 from Nω-phosphoarginine residues of phosphopeptides. These results indicate that both phosphatases function as protein arginine phosphatases in different manners, and thatNω-phosphoarginine phosphatase is useful for selectively detecting Nω-phosphoarginine residue in peptides containing various kinds of phosphorylated amino acids. © by the Journal of Biochemistry Regular Papers nationallicence alkaline phosphatase nationallicence Nω-phosphoarginine phosphatase nationallicence phenylglyoxal treatment nationallicence 31P-NMR nationallicence protein arginine phosphatase nationallicence Kumon Akira Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut Kodama Hiroaki Department of Chemistry, Faculty of Science and Engineering, Saga University Honjyo 1, Saga, Saga 840 aut Kondo Michio Department of Chemistry, Faculty of Science and Engineering, Saga University Honjyo 1, Saga, Saga 840 aut Yokoi Fumiaki Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut Hiraishi Hiroyuki Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 719-724 0021-924X 119:4<719 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021301 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021301 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kumon Akira Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut NATIONALLICENCE 700 1- Kodama Hiroaki Department of Chemistry, Faculty of Science and Engineering, Saga University Honjyo 1, Saga, Saga 840 aut NATIONALLICENCE 700 1- Kondo Michio Department of Chemistry, Faculty of Science and Engineering, Saga University Honjyo 1, Saga, Saga 840 aut NATIONALLICENCE 700 1- Yokoi Fumiaki Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut NATIONALLICENCE 700 1- Hiraishi Hiroyuki Department of Biochemistry, Saga Medical School Nabeshima 5-1-1, Saga, Saga 849 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 719-724 0021-924X 119:4<719 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford