Kinetic analysis of γ-glutamyltransferase reaction process for measuring activity via an integration strategy at low concentrations of γ-glutamyl p-nitroaniline
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Atkins, G.L., Nimmo, I.A., 1973. The reliability of Michaelis-Menten constants and maximum velocities estimated by using the integrated Michaelis-Menten equation. Biochem. J., 135(3):779–784.
Castonguay, R., Halim, D., Morin, M., Furtos, A., Lherbet, C., Bonneil, E., Thibault, P., Keillor, J.W., 2007. Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human γ-glutamyl-transpeptidase. Biochemistry, 46(43):12253–12262. [doi: 10.1021/bi700956c]
Cook, N.D., Peters, T.J., 1986. The simultaneous hydrolysis of glutathione and glutamine by rat kidney γ-glutamyltransferase. Biochim. Biophys. Acta, 884(1):207–210.
Cook, N.D., Upperton, K.P., Challis, B.C., Peters, T.J., 1987. The donor specificity and kinetics of the hydrolysis reaction of γ-glutamyltransferase. Biochim. Biophys. Acta, 914(3):240–245. [doi:10.1016/0167-4838(87)90283-4]
Dvorakova, L., Krusek, J., Stastny, F., Lisy, V., 1996. Analysis of kinetic properties of γ-glutamyl transpeptidase from rat kidney. Gen. Physiol. Biophys., 15(5):403–413.
Fossati, P., Melzi d’Eril, G.V., Tarenghi, G., Prencipe, L., Berti, G., 1986. A kinetic colorimetric assay of γ-glutamyl-transferase. Clin. Chem., 32 (8):1581–1584.
Gella, F.J., Gubern, G., Vidal, R., Canalias, F., 1997. Determination of total and pancreatic α-amylase in human serum with 2-chloro-4-nitrophenyl-α-D-maltotrioside as substrate. Clin. Chim. Acta, 259(1–2):147–160 [doi:10.1016/S0009-8981(96)06481-9]
Giral, P., Jacob, N., Dourmap, C., Hansel, B., Carrié, A., Bruckert, E., Girerd, X., Chapman, M.J., 2008. Elevated γ-glutamyltransferase activity and perturbed thiol profile are associated with features of metabolic syndrome. Arterioscler. Thromb. Vasc. Biol., 28(3):587–593. [doi:10.1161/ATVBAHA.107.157891]
Jo, S.K., Lee, W.Y., Rhee, E.J., Won, J.C., Jung, C.H., Park, C.Y., Oh, K.W., Park, S.W., Kim, S.W., 2009. Serum γ-glutamyl transferase activity predicts future development of metabolic syndrome defined by 2 different criteria. Clin. Chim. Acta, 403(1–2):234–240. [doi:10.1016/j.cca.2009.03.035]
Liao, F., Liu, W.L., Zhou, Q.X., Zeng, Z.C., Zuo, Y.P., 2001. Assay of serum arylesterase activity by fitting to the reaction curve with an integrated rate equation. Clin. Chim. Acta, 314(1–2):67–76. [doi:10.1016/S0009-8981(01)00631-3]
Liao, F., Tian, K.C., Yang, X., Zhou, Q.X., Zeng, Z.C., Zuo, Y.P., 2003. Kinetic substrate quantification by nonlinear fitting reaction curve to integrated Michaelis-Menten equation. Anal. Bioanal. Chem., 375(6):756–762.
Liao, F., Zhu, X.Y., Wang, Y.M., Zuo, Y.P., 2005. The comparison of the estimation of enzyme kinetic parameters by fitting reaction curve to the integrated Michaelis-Menten rate equations of different predictor variables. J. Biochem. Biophys. Methods, 62(1):13–24. [doi:10.1016/j.jbbm.2004.06.010]
Liao, F., Zhao, Y.S., Zhao, L.N., Tao, J., Zhu, X.Y., Liu, L., 2006. The evaluation of a direct kinetic method for serum uric acid assay by predicting the background absorbance of uricase reaction solution with an integrated method. J. Zhejiang Univ.-Sci. B, 7(6):497–502. [doi:10.1631/jzus.2006.B0497]
Liao, F., Zhao, L.N., Zhao, Y.S., Tao, J., Zuo, Y.P., 2007. Integrated rate equation considering product inhibition and its application to kinetic assay of serum ethanol. Anal. Sci., 23(4):439–444. [doi:10.2116/analsci.23.439]
Liao, F., Yang, D.Y., Tang, J.Q., Yang, X.L., Liu, B.Z., Zhao, Y.S., Zhao, L.N., Liao, H., Yu, M.A., 2009. The measurement of serum cholinesterase activities by an integration strategy with expanded linear ranges and negligible substrate-activation. Clin. Biochem., 42(9):926–928. [doi: 10.1016/j.clinbiochem.2008.11.016]
Lim, J.S., Lee, D.H., Park, J.Y., Jin, S.H., Jacobs, D.R., 2007. A strong interaction between serum γ-glutamyltransferase and obesity on the risk of prevalent type 2 diabetes: results from the third national health and nutrition examination survey. Clin. Chem., 53(6):1092–1098. [doi:10.1373/clinchem.2006.079814]
Liu, B.Z., Zhao, Y.S., Zhao, L.N., Xie, Y.L., Zhu, S., Li, Z.R., Liu, Y., Lu, W., Yang, X.L., Xie, G.M., et al., 2009. An integration strategy to estimate the initial rates of enzyme reactions with much expanded linear ranges using uricases as models. Anal. Chim. Acta, 631(1):22–28. [doi:10.1016/j.aca.2008.10.021]
London, J.W., Shaw, L.M., Fetterolf, D., Garfinkel, D., 1976. Determination of the mechanism and kinetic constants for hog kidney γ-glutamyltransferase. Biochem. J., 157(3):609–617.
Newman, P.F.J., Atkins, G.L., Nimmo, I.A., 1974. The effects of systematic error on the accuracy of Michaelis constant and maximum velocities estimated by using the integrated Michaelis-Menten equation. Biochem. J., 143(3): 779–781.
Orsi, B.A., Tipton, K.F., 1979. Kinetic analysis of progress curves. Methods Enzymol., 63:159–183. [doi:10.1016/0076-6879(79)63010-0]
Ruttmann, E., Brant, L.J., Concin, H., Diem, G., Rapp, K., Ulmer, H., 2005. γ-Glutamyltransferase as a risk factor for cardiovascular disease mortality. An investigation in a cohort of 163 944 Austrian adults. Circulation, 112(14): 2130–2137. [doi:10.1161/CIRCULATIONAHA.105.552547]
Shaw, L.M., London, J.W., Fetterolf, D., Garfinkel, D., 1972. γ-Glutamyltransferase: kinetic properties and assay conditions when γ-glutamyl-4-nitroanilide and its 3-carboxy derivative are used as donor substrates. Clin. Chem., 23(1):79–85.
Stein, R.L., DeCicco, C., Nelson, D., Thomas, B., 2001. Slow-binding inhibition of γ-glutamyl transpeptidase by γ-boroGlu. Biochemistry, 40(19):5804–5811. [doi:10.1021/bi010147i]
Tsao, F.H., Shanmuganayagam, D., Zachman, D.K., Khosravi, M., Folts, J.D., Meyer, K.C., 2007. A continuous fluorescence assay for the determination of calcium-dependent secretory phospholipase A2 activity in serum. Clin. Chim. Acta, 379(1–2):119–123. [doi:10.1016/j.cca.2006.12.023]
Turgut, O., Yilmaz, A., Yalta, K., Karadas, F., Birhan, Y.M., 2006. γ-Glutamyltransferase is a promising biomarker for cardiovascular risk. Med. Hypotheses, 67(5):1060–1064. [doi:10.1016/j.mehy.2006.04.010]
Walsh, R., Martin, E., Darvesh, S., 2010. A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters. Biochim. Biophys. Acta, 1800(1):1–5.
Whitfield, J.B., 2001. γ-Glutamyl transferase. Crit. Rev. Clin. Lab. Sci., 38(4):263–355. [doi:10.1080/20014091084227]
Winn-Deen, E.S., David, H., Sigler, G., Chavez, R., 1988. Development of a direct assay for alpha-amylase. Clin. Chem., 34(10):2005–2008.
Yamada, M., Fujita, T., 2007. New procedure for the measurement of pancreatic lipase activity in human serum using a thioester substrate. Clin. Chim. Acta, 383(1–2): 85–90. [doi:10.1016/j.cca.2007.04.021]