Enzymatic synthesis of polyprenol monophosphate mannose in insects

Mostrar otras versiones (1)

The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Belocopitow, E.
Otros Autores: Marechal, L.R, Quesada Allue, L.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Kluwer Academic Publishers 1977
Acceso en línea:Registro en Scopus
DOI
Handle
Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
LEADER 07274caa a22010337a 4500
001 PAPER-12308
003 AR-BaUEN
005 20230518204230.0
008 190411s1977 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-0017409847 
024 7 |2 cas  |a dolichol phosphate, 12698-55-4, 34457-14-2; mannose, 31103-86-3, 3458-28-4; Cobalt, 7440-48-4; Hexosephosphates; Hexosyltransferases, EC 2.4.1.-; Magnesium, 7439-95-4; Manganese, 7439-96-5; Mannosyltransferases, EC 2.4.1.; Phospholipids; Polyethylene Glycols; Terpenes 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a MCBIB 
100 1 |a Belocopitow, E. 
245 1 0 |a Enzymatic synthesis of polyprenol monophosphate mannose in insects 
260 |b Kluwer Academic Publishers  |c 1977 
270 1 0 |m Belocopitow, E.; Instituto de Investigaciones Bioquimicas 'Fundación Campomar', and Facultad de Ciencias Exactas y Naturales, Obligado 2490, Buenos Aires, 1428, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Hemming, F.N., (1973) Biochemistry Series One, pp. 39-97. , H. L., Kornberg, D. C., Phillips, T. W., Goodwin, London and University Park Press, Baltimore, Butterworths 
504 |a Behrens, N.H., (1974) Biology and Chemistry of Eucaryotic Cell Surfaces, pp. 159-178. , E., Lee, E., Smith, Academic Press, New York 
504 |a Lennarz, W.J., (1975) Science, 188, pp. 986-991 
504 |a Parodi, A.J., Leloir, (1976) T.I.B.S., 1, pp. 58-59 
504 |a Quesada Allué, L.A., Belocopitow, E., Marechal, L.R., Glycosyl transfer to an acceptor lipid from insects (1975) Biochemical and Biophysical Research Communications, 66, pp. 1201-1208 
504 |a Behrens, N.H., Leloir, L.F., (1970) Proc. Nat. Acad. Sci. U.S.A., 66, pp. 153-159 
504 |a Quesada Allué, L.A., Marechal, L.R., Belocopitow, E., (1976) FEBS Lett., 67, pp. 243-247 
504 |a Folch, J., Lees, M., Sloane, S.G., (1957) J. Biol. Chem., 226, pp. 497-509 
504 |a Porter, C., Jaworski, E., (1965) J. Insect Physiol, 11, pp. 1151-1160 
504 |a Lowry, O., Rosebrough, N.J., Farr, A.L., Randall, R.J., (1951) J. Biol. Chem., 193, pp. 265-275 
504 |a Kates, M., (1972) Laboratory Techniques in Biochemistry and Molecular Biology, pp. 267-601. , T. S., Work, E., Work, North-Holland Publishing Co., Amsterdam-London 
504 |a Trevelyan, W.E., Procter, D.P., Harrison, J.S., (1950) Nature, 166, pp. 444-445 
504 |a Bray, G.A., (1960) Anal. Biochem., 1, pp. 279-285 
504 |a Tkacz, J.H., Herscovics, A., Warren, C., Jeanloz, R., (1974) J. Biol. Chem., 249, pp. 6372-6381 
504 |a Wedgwood, J.F., Strominger, J.L., Warren, C., (1974) J. Biol. Chem., 249, pp. 6316-6324 
504 |a Adamany, A., Spiro, R.G., (1975) J. Biol. Chem., 250, pp. 2842-2854 
504 |a Butler, N., Wolf, G., (1976) Biochem. Biophys. Res. Commun., 68, pp. 704-711 
504 |a Waechter, C.J., Lucas, J.J., Lennarz, J.W., (1973) J. Biol. Chem., 248, pp. 7570-7579 
504 |a Martin, H.G., Thorn, J.I.K., (1974) Biochem. J., 138, pp. 281-289 
504 |a Vessey, D.A., Zakim, D., (1975) Eur. J. Biochem., 53, pp. 499-504 
504 |a Tanner, W., (1969) Biochem. Biophys. Res. Commun., 35, pp. 144-150 
504 |a Villemez, C.L., Clark, A.F., (1969) Biochem. biophys. Res. Commun., 36, pp. 57-63 
504 |a Hassid, W.Z., (1972) Biochemistry of the Glycosidic Linkage, pp. 315-335. , R., Piras, H., Pontis, Academic Press, New York 
504 |a Rouser, G., Krischevsky, G., Yamamoto, A., (1967) Lipid Chromatographic Analysis, pp. 99-162. , G. V., Marinetti, Marcel Dekker Inc., New York 
504 |a Tkacz, J.S., Lampen, O., (1975) Biochem. Biophys. Res. Commun., 65, pp. 248-257 
504 |a Sweeley, C.C., (1969) Methods in Enzymology, pp. 254-267. , J. M., Lowenstein, Academic Press, New York and London 
504 |a García, R.G., Recondo, E., Dankert, M., (1974) Eur. J. Biochem., 43, pp. 93-105 
504 |a Behrens, N.H., Parodi, A., Leloir, L.F., (1971) Proc. Nat. Acad. Sci. U.S.A., 68, pp. 2857-2860 
504 |a Herndon, W.C., (1967) J. Chem. Educ., 44, pp. 724-727 
504 |a Herscovics, A., Warren, C.D., Jeanloz, R.W., Wedgewood, J.F., Strominger, J.L., (1974) FEBS Lett., 45, pp. 312-317 
504 |a Beedle, A.S., Walton, M.J., Goodwin, T., (1975) Insect Biochem., 5, pp. 465-472 
520 3 |a The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton X-100 and magnesium ions, the optimal concentration of the latter being 10mM. The optimal temperature of the reaction was 25 °C and the maximal activity was obtained at pH 7.9. The mannolipid formed behaved as a monophosphodiester when chromatographed on DEAE-cellulose. Weak acid treatment of the product liberated mannose. Its behaviour both on thin layer and Sephadex G-150 chromatography would indicate the presence of a number of isoprenyl units similar to the dolichol and different from the ficaprenol derivative. Stability to phenol treatment indicated that the lipid fraction of the mannolipid is an ±-saturated polyprenol phosphate similar to dolichol monophosphate. © 1977 Dr. W. Junk b.v. Publishers.  |l eng 
593 |a Instituto de Investigaciones Bioquimicas 'Fundación Campomar', and Facultad de Ciencias Exactas y Naturales, Obligado 2490, Buenos Aires, 1428, Argentina 
690 1 0 |a DOLICHOL PHOSPHATE 
690 1 0 |a MANNOSE 
690 1 0 |a ARTHROPOD 
690 1 0 |a IN VITRO STUDY 
690 1 0 |a MICROSOME 
690 1 0 |a POLYPRENYL PHOSPHATE 
690 1 0 |a THEORETICAL STUDY 
690 1 0 |a ANIMAL 
690 1 0 |a COBALT 
690 1 0 |a DIPTERA 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a HEXOSEPHOSPHATES 
690 1 0 |a HEXOSYLTRANSFERASES 
690 1 0 |a HYDROGEN-ION CONCENTRATION 
690 1 0 |a KINETICS 
690 1 0 |a LARVA 
690 1 0 |a MAGNESIUM 
690 1 0 |a MANGANESE 
690 1 0 |a MANNOSYLTRANSFERASES 
690 1 0 |a MICROSOMES 
690 1 0 |a PHOSPHOLIPIDS 
690 1 0 |a POLYETHYLENE GLYCOLS 
690 1 0 |a PUPA 
690 1 0 |a TEMPERATURE 
690 1 0 |a TERPENES 
690 1 0 |a TRIATOMA 
690 1 0 |a TRIATOMINAE 
700 1 |a Marechal, L.R. 
700 1 |a Quesada Allue, L.A. 
773 0 |d Kluwer Academic Publishers, 1977  |g v. 16  |h pp. 127-134  |k n. 2-3  |p Mol Cell Biochem  |x 03008177  |w (AR-BaUEN)CENRE-3498  |t Molecular and Cellular Biochemistry 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017409847&doi=10.1007%2fBF01732053&partnerID=40&md5=9fb6ff26b8127fb3ce191cbc66353cfc  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1007/BF01732053  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p127_Belocopitow  |y Registro en la Biblioteca Digital 
961 |a paper_03008177_v16_n2-3_p127_Belocopitow  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
963 |a VARI 
999 |c 73261 

Ejemplares similares