Purification and Characterization of a Low-Molecular-Weight Bovine Kidney Acid Phosphatase

Anais da Academia Brasileira de Ciencias

Volumn 69, Issue 4, 1997, Pages 451-460

  Granjeiro, José M ^a   Taga, Eulazio M ^b   Aoyama, Hiroshi ^a  

^a UNIVERSITY OF CAMPINAS   (Brazil)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Acid phosphatase; Effectors; Kinetics; O vanadate inhibition; Purification; Pyridoxal 5 phosphate inhibition

Indexed keywords

BOVINAE;

ACID PHOSPHATASE; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ISOLATION AND PURIFICATION; KIDNEY; KINETICS; MOLECULAR WEIGHT;

ACID PHOSPHATASE; ANIMALS; CATTLE; INDICATORS AND REAGENTS; KIDNEY; KINETICS; MOLECULAR WEIGHT; SUBSTRATE SPECIFICITY;

EID: 0031311392     PISSN: 00013765     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (40)

1. ARAÚJO, P. S.; MIES, V. & MIRANDA, O., (1976), Subcelular distribution of low-molecular-weight acid phosphatases. Biochim. Biophys. Acta, 452: 121-130.
2. BALDIJÃO, C. E. M.; GUIJA, E.; BITTENCOURT, H. M. S, & CHAIMOVICH, H., (1975), Steady state kinetics and effects of inhibitors on acid phosphatase from bovine brain. Biochim. Biophys. Acta, 391: 316-325.
3. BHARGAVA, R. & SACHAR, R. C., (1987), Induction of acid phosphatase in cotton seedlings enzyme purification, subunit structure and kinetic properties. Phytochemistry, 26: 1293-1297.
4. BAXTER, J, H. & SUELTER, C. H., (1985), Resolution of the low-molecular-weight acid phosphatase in avian pectoral muscle into distinct enzyme forms. Arch. Biochem. Biophys., 239: 29-37.
5. BERTI, A; RIGACCI, S.; RAUGEI, G.; DEGL'INNOCENTI, D. & RAMPONI, G., (1994), Inhibition of cellular esponse to platelet-derived growth factor by low Mr phosphotyrosine protein phosphatase overexpression. FEBS Lett., 349: 7-12.
6. CAMICI, G.; MANAO, G.; CAPPUGI, G.; MODESTI, A.; STEFANI, M. & RAMPONI, G., (1989), The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase. J. Biol. Chem., 264: 2560-2567.
7. CHAIMOVICH, H. & NOME, F., (1970), Purification and properties of an acid phosphatase from bovine brain. Arch. Biochem. Biophys., 139: 9-16.
8. CHERNOFF, J. & LI, H. C., (1985), A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase. Arch. Biochem. Biophys., 240: 135-145.
9. CHIARUGI, P.; MARZOCCHINI, R.; RAUGEI, G.; PAZZAGLI, C.; BERTI, A.; CAMICI, G.; MANAO, G.; CAPPUGI, G. & RAMPONI, G., (1992), Differential role of four cysteines residues on the activity of a low Mr phosphotyrosine protein phosphatase. FEBS Lett., 310: 9-12.
10. CHIARUGI, P.; CIRRI, P.; CAMICI, G.; MANAO, G; FIASCHI, T.; RAUGEI, G.; CAPPUGI, G. & RAMPONI, G., (1994), The role of His66 and His72 in the reaction mechanism of bovine low-Mr phosphotyrosine protein phosphatase. Biochem. J., 298: 427-433.
11. CHIARUGI, P.; CIRRI, P.; RAUGEI, G.; CAMICI, G.; DOLFI, F.; BERTI, A. & RAMPONI, G., (1995), PDGF receptor as a specific in vivo target for low Mr phosphotyrosine protein phosphatase. FEBS Lett., 372: 49-53.
12. DAVIS, J. P.; ZHOU, M.-M. & VAN ETTEN, R. L., (1994), Kinetic and site directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase. J. Biol. Chem., 269: 8734-8740.
13. DE-KUNDU, P. & BANERJEE, A. C., (1990), Multiple forms of acid phosphatase from seedlings axes of Vigna radiata. Phytochemistry, 29: 2825-2828.
14. DISSING, J. & SVENSMARK, O., (1990), Human red cell acid phosphatase: purification and properties of the A, B and C isoenzymes. Biochim. Biophys. Acta, 1041: 232-242.
15. DISSING, J. & JOHNSEN, A. H., (1992), Human red cell acid phosphatase (ZCP1): the primary structure of two pairs of isoenzymes encoded by the ACP1*A and ACP1*C alleles. Biochim. Biophys. Acta, 1121: 261-268.
16. DISSING, J.; RANGAARD, B. & CHRISTENSEN, U., (1993), Activity modulation of the fas and slow isoenzymes of human cytosolic low-molecular-weight acid phosphatase (ACP1) by purines. Biochim. Biophys. Acta, 1162: 275-282.
17. rd Edn, Academic Press, New York, p. 1116.
18. DUFF, S. M. G.; SARATH, G. & PLAXTON, W. C., (1994), The role of acid phosphatases in plant phosphorus metabolism. Physiol. Plant., 90: 791-800.
19. FAUMAN, E. B. & SAPER, M. A., (1996), Structure and function of the protein tyrosine phosphatase. Trends Biochem. Sci., 21: 413-417.
20. FUCHS, K. R.; SHEKELS, L. L. & BERNLOHR, D. A., (1992), Analysis of the ACP1 gene product: classification as an FMN phosphatase. Biochem. Biophys. Res. Commun., 189: 1598-1605.
21. FUJIMOTO, S.; URATA, Y.; NAKAGAWA, T. & OHARA, A., (1984), Characterization of intermediate-molecular-weight acid phosphatase from bovine kidney cortex. J. Biochem., 96: 1079-1088.
22. GALKA, M.; DZIEMBOR-GRYSZKIEWICZ, E.; Kos, S. & OSTROWSKI, W., (1980), Properties of low-molecular-weight acid phosphatases isolated from cytosol and chromatin of rat liver. Acta Biochim. Pol., 27: 281-293.
23. HOLLANDER, V. P., (1971), Acid phosphatases. In: BOYER, P. D. ed. The Enzymes. New York, Academic Press, p. 449-455.
24. KLARLUND, J. K., (1985), Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins. Cell, 41: 707-717.
25. KUMAGAI, A. & DUNPHY, W. G., (1991), The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell, 64: 903-914.
26. LOGAN, T. M.; ZHOU, M-M.; NETTESHEIM, D. G.; MEADOWS, R. P.; VAN ETTEN, R. L. & FESIK, S. W., (1994), Solution structure of a low molecular weight protein tyrosine phosphatase. Biochemistry, 33: 11087-11096.
27. LOWRY, O. H. & LOPEZ, J., (1946), The determination of inorganic phosphate in the presence of labile phosphate esters. J. Biol. Chem., 162: 421-424.
28. LOWRY, O. H.; ROSEBROUGH, N.; FARR, A. & RANDAL, R., (1951), Protein measurement with the phenol reagent. J. Biol. Chem., 193: 265-275.
29. 2+-dependent acid phosphatase form. Int. J. Biochem., 24: 1619-1623.
30. POT, D. A. & DIXON, J. E., (1992), A thousand and two protein tyrosine phosphatases. Biochim. Biophys. Acta, 1136: 35-43.
31. RAMPONI, G.; MANAO, G.; CAMICI, G.; CAPPUGI, G.; RUGGIERO, M. & BOTTARO, G. P., (1989), The 18 kDa cytosolic acid phosphatase from bovine liver has phosphotyrosine activity on the autophosphorylated epidermal growth factor receptor. FEBS Lett., 250: 469-473.
32. REISFELD, R. A.; LEWIS, V. J. & WILLIAMS, D. E., (1962), Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature, 195: 281-283.
33. SAEED, A.; TREMORI, E.; MANAO, G.; CAMICI, G.; CAPPUGI, G. & RAMPONI, G., (1990), Bovine brain low Mr acid phosphatase: purification and properties. Physiol. Chem. Phys. and Med. NMR, 22: 81-94.
34. SU, X.-D.; TADDEI, N.; STEFANI, M.; RAMPONI, G. & NORDLUND, P., (1994), The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature, 370: 575-578.
35. TAGA, E. M. & VAN ETTEN, R. L., (1982), Human liver acid phosphatase: purification and properties of a low molecular weight isoenzymes. Arch. Biochem. Biophys., 214: 505-515.
36. TANTZAKI, M. M.; BITTENCOURT, H. M. S. & CHAIMOVICH, H., (1976), Activation of low molecular weight acid phosphatase from bovine brain by purines and glycerol. Biochim. Biophys. Acta, 485: 116-123.
37. ULLAH, A. H. J. & GIBSON, D. M., (1988), Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds. Arch. Biochem. Biophys., 260: 514-520.
38. WAHEED, A.; LAIDLER, P. M.; WO, Y.-Y. P. & VAN ETTEN, R. L., (1988), Purification and physicochemical characterization of a human placental acid phosphatase activity. Biochemistry, 27: 4265-4273.
39. WEBER, K. & OSBORN, M., (1969), The reability of molecular weight determination by sodium dodecyl sulfate-polyacrilamide gel electrophoresys. J. Biol. Chem., 244: 4406-4412.
40. ZHANG, Z.-Y. & VAN ETTEN, R. L, (1990), Purification and characterization of a low-molecular-weight acid phosphatase - a phosphotyrosyl-protein phosphatase from bovine heart. Arch. Biochem. Biophys., 282: 39-49.