Dolichyl‐Phosphate Phosphatase and Dolichyl‐Diphosphate Phosphatase in Rat‐Liver Microsomes

Dolichyl‐phosphate phosphatase and dolichyl‐diphosphate phosphatase activities of a liver‐cell microsomal preparation were solubilized by treatment with Triton X‐100. The I00000 × g supernatant was then passed through a column of Sepharose‐4B – concanavalin A. Both enzyme activities were found in th...

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Autor principal: BELOCOPITOW, E.
Otros Autores: BOSCOBOINIK, D.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1982
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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024 7 |2 scopus  |a 2-s2.0-0019960705 
024 7 |2 cas  |a dolichyl-phosphatase, EC 3.1.3.51; dolichyldiphosphatase, EC 3.6.1.43; Phosphodiesterase Inhibitors; Phospholipids; Phosphoric Monoester Hydrolases, EC 3.1.3; Pyrophosphatases, EC 3.6.1.- 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a BELOCOPITOW, E. 
245 1 0 |a Dolichyl‐Phosphate Phosphatase and Dolichyl‐Diphosphate Phosphatase in Rat‐Liver Microsomes 
260 |c 1982 
270 1 0 |m BELOCOPITOW, E.; Instituto de Investigaciones Bioquímicas 'Fundacion Campomar', Obligado, Buenos Aires, RA-1428, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Parodi, A.J., Leloir, L.F., (1979) Biochim. Biophys. Acta, 559, pp. 1-37 
504 |a Waechter, C.J., Lennarz, W.J., (1976) Annu, Rev. Biochem., 45, pp. 95-112 
504 |a Hemming, F.W., (1977) Biochem. Soc. Trans., 5, pp. 1223-1231 
504 |a Lucas, J.J., Levine, E., (1977) J. Biol. Chem., 252, pp. 4330-4336 
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504 |a Carson, D.D., Lennarz, W.J., (1981) J. Biol. Chem., 256, pp. 4679-4686 
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504 |a Allen, M.C., Kalin, J.R., Jr., Sack, J., Verizzo, D., (1978) Biochemistry, 17, pp. 5020-5026 
504 |a Burton, W.A., Scher, M.G., Waechter, C.J., (1979) J. Biol. Chem., 254, pp. 632-635 
504 |a Rip, J.W., Carrol, K.K., (1980) Can. J. Biochem., 58, pp. 1051-1056 
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504 |a Idoyaga‐Vargas, V., Belocopitow, E., Mentaberry, A., Carminatti, H., A phosphatase acting on dolichyl phosphate in membranes from neuronal perikarya (1980) FEBS Letters, 112, pp. 63-65 
504 |a Kato, S., Tsuji, M., Nakanishi, Y., Suzuki, S., (1980) Biochem. Biophys. Res, Commun, 95, pp. 770-776 
504 |a Rip, J.W., Rupar, A.C., Chaudhary, N., Carrol, K.K., (1981) J. Biol. Chem., 256, pp. 1929-1934 
504 |a Burton, W.A., Scher, M.G., Waechter, C.J., (1981) Arch. Biochem. Biophys, 208, pp. 409-417 
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504 |a Cuatrecasas, P., (1970) J. Biol. Chem., 245, pp. 3059-3065 
504 |a Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., (1951) J. Biol. Chem., 193, pp. 265-275 
504 |a Boscoboinik, D.O., Belocopitow, E., (1981) Anal. Biochem., 114, pp. 42-45 
504 |a Parodi, A.J., Mordoh, J., Krisman, C.R., Leloir, L.F., (1969) Arch. Biochem. Biophys., 132, pp. 111-117 
504 |a Keenan, F.W., Kruczek, M., (1975) Anal. Biochem., 69, pp. 504-509 
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504 |a Rouser, G., Kritchevsky, G., Yamamoto, A., (1967) Lipid Chromatographic Analysis, 1, pp. 99-162. , Dekker, N. Y 
504 |a Colbeau, A., Nechbaur, J., Vignais, P.M., (1971) Biochem. Biophys. Acta, 249, pp. 462-492 
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504 |a Daleo, G.R., Hopp, H.E., Romero, P.A., Pont Lezica, R., (1977) FEBS Lett., 81, pp. 411-414 
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504 |a Rupar, C.A., Carrol, K.K., (1978) Lipids, 13, pp. 291-293 
520 3 |a Dolichyl‐phosphate phosphatase and dolichyl‐diphosphate phosphatase activities of a liver‐cell microsomal preparation were solubilized by treatment with Triton X‐100. The I00000 × g supernatant was then passed through a column of Sepharose‐4B – concanavalin A. Both enzyme activities were found in the percolate. This treatment eliminated inhibition by ATP and glucose 6‐phosphate in both phosphatase activities. In each case the activities were inhibited by higher concentrations of enzyme preparation due to the presence of phospho‐ lipids. The inhibitory effects of either phosphatidylcholine or phosphatidylethanolamine were due to competition for detergent. On the other hand, the effect produced by phosphatidic acid appeared to be different, since it did not change the optimal concentration of Triton X‐100 for the two enzymes. Dolichyl‐phosphate phosphatase was strongly inhibited by both Pi and PPi, whereas dolichyl‐diphosphate phosphatase was only slightly inhibited by Pi and not at all by PPi. Dolichyl‐diphosphate phosphatase was more inhibited by divalent cations than dolichyl‐phosphate phos‐ phatase. The apparent Km of dolichyl‐phosphate phosphatase for dolichyl phosphate was 0.15 mM. Dolichol also inhibited dolichyl‐phosphate phosphatase, but it produced a stronger inhibition on dolichyl‐diphosphate phosphatase. The inhibitory effect of dolichol was not entirely due to detergent competition. Copyright © 1982, Wiley Blackwell. All rights reserved  |l eng 
593 |a Instituto de Investigaciones Bioquímicas 'Fundacion Campomar', Obligado, Buenos Aires, RA-1428, Argentina 
690 1 0 |a ENZYME 
690 1 0 |a ANIMAL EXPERIMENT 
690 1 0 |a DOLICHOL DIPHOSPHATASE 
690 1 0 |a DOLICHYL PHOSPHATASE 
690 1 0 |a LIVER 
690 1 0 |a LIVER MICROSOME 
690 1 0 |a RAT 
690 1 0 |a ANIMAL 
690 1 0 |a HYDROGEN-ION CONCENTRATION 
690 1 0 |a KINETICS 
690 1 0 |a MICROSOMES, LIVER 
690 1 0 |a PHOSPHODIESTERASE INHIBITORS 
690 1 0 |a PHOSPHOLIPIDS 
690 1 0 |a PHOSPHORIC MONOESTER HYDROLASES 
690 1 0 |a PYROPHOSPHATASES 
690 1 0 |a RATS 
690 1 0 |a SUBSTRATE SPECIFICITY 
690 1 0 |a TEMPERATURE 
700 1 |a BOSCOBOINIK, D. 
773 0 |d 1982  |g v. 125  |h pp. 167-173  |k n. 1  |p Eur. J. Biochem.  |x 00142956  |w (AR-BaUEN)CENRE-3060  |t European Journal of Biochemistry 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00142956_v125_n1_p167_BELOCOPITOW  |y Handle 
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