Artículos de revistas
Bovine Kidney Low Molecular Weight Acid Phosphatase: Fmn-dependent Kinetics
Registro en:
Biochemistry And Molecular Biology International. , v. 41, n. 6, p. 1201 - 1208, 1997.
10399712
2-s2.0-0030976268
Autor
Granjeiro J.M.
Ferreira C.V.
Juca M.B.
Taga E.M.
Aoyama H.
Institución
Resumen
A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p-nitrophenyl phosphate- (45.44 kJ mol-1) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2 and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction. 41 6 1201 1208 Hollander, V.P., (1971) The Enzymes, 4, pp. 449-455. , Boyer, PD ed., Academic Press, New York Panara, F., Angiolillo, A., Fagotti, A., Di Rosa, I., Francesca, S., Pascolini, R., (1992) Int. J. Biochem., 24, pp. 1619-1623 De Araújo, P.S., Mies, V., Miranda, O., (1976) Biochim. Biophys. Acta, 452, pp. 121-130 Zhang, Z.-Y., Van Etten, R.L., (1990) Arch. Biochem. Biophys., 282, pp. 39-49 Davis, J.P., Zhou, M.-M., Van Etten, R.L., (1994) J. Biol. Chem., 269, pp. 8734-8740 Chiarugi, P., Cirri, P., Camici, G., Manao, G., Fiaschi, T., Raugei, G., Cappugi, G., Ramponi, G., (1994) Biochem. J., 298, pp. 427-433 Logan, T.M., Zhou, M.-M., Nettesheim, D.G., Meadows, R.P., Van Etten, R.L., Fesik, S.W., (1994) Biochemistry, 33, pp. 11087-11096 Su, X.-D., Taddei, N., Stefani, M., Ramponi, G., Nordlund, P., (1994) Nature, 370, pp. 575-578 Chernoff, J., Li, H.C., (1985) Arch. Biochem. Biophys., 240, pp. 135-145 Berti, A., Rigacci, S., Raugei, G., Degl'Innocenti, D., Ramponi, G., (1994) FEBS Lett., 349, pp. 7-12 Chiarugi, P., Cirri, P., Raugei, G., Camici, G., Dolfi, F., Berti, A., Ramponi, G., (1995) FEBS Lett., 372, pp. 49-53 Iaga, E.M., Van Etten, R.L., (1982) Arch. Biochem. Biophys., 214, pp. 505-515 Lowry, O.H., Lopez, J., (1946) J. Biol. Chem., 162, pp. 421-424 Zhang, Z.-Y., Van Etten, R.L., (1991) J. Biol. Chem., 266, pp. 1516-1525 Lowry, O.H., Rosebrough, N., Fan, A., Randal, R., (1951) J. Biol. Chem., 193, pp. 265-775 Fuchs, K.R., Shekels, L.L., Bernlohr, D.A., (1992) Biochem. Biophys. Res. Commun., 189, pp. 1598-1605 Miernyk, J.A., (1992) Phytochemistry, 31, pp. 2613-2616 Dixon, M., Webb, E.C., (1979) Enzymes (3rd Edn), 47, pp. 169-181. , Academic Press, New York Brandâo, M.E.G., Aoyama, H., (1992) Plant Physiol. Biochem., 30, pp. 753-760 Galka, M., Dziembor-Gryszkiewicz, E., Kos, S., Ostrowski, W., (1980) Acta Biochim. Pol, 27, pp. 281-293 Janska, H., Kubicz, A., Bem, M., Van Etten, R.E., (1986) Comp. Biochem. Physiol., 85 B, pp. 753-758 Fujimoto, S., Urata, Y., Nakagawa, T., Ohara, A., (1984) J. Biochem., 96, pp. 1079-1088 Tanizaki, M.M., Bittencourt, H.M.S., Chaimovich, H., (1976) Biochim. Biophys. Acta, 485, pp. 116-123 Baldijão, C.E.M., Guija, E., Bittencourt, H.M.S., Chaimovich, H., (1975) Biochim. Biophys. Acta, 391, pp. 316-325 Chiarugi, P., Marzocchini, R., Raugei, G., Pazzagli, C., Berti, A., Camici, G., Manao, G., Ramponi, G., (1992) FEBS Lett., 310, pp. 9-12 Pot, D.A., Dixon, J.E., (1992) Biochim. Biophys. Acta, 1136, pp. 35-43