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Abstract:

We have examined β-D-galactofuranosidase production by Penicillium fellutanum in the presence of D-galactono-1,4-lactone or 4-aminophenyl 1-thio-β-D-galactofuranoside, two potent in vitro inhibitors of the enzyme. Activity of the enzyme in the culture filtrate was increased by 35% when glucose was replaced by D-galactose as the carbon source, and the activity diminished 80% of the control value when the inhibitors were added. Significant alterations of the culture were observed: (a) the medium became increasingly opalescent due to the secretion of a protein aggregate (PA) which contained 15% neutral sugar, mainly ribose; (b) the peptidophosphogalactomannan (pPGM) containing galactofuranose, normally produced by P. fellutanum, could not be obtained from the culture medium in the presence of the inhibitors; (c) the content of galactofuranose in the cell wall was significantly decreased in the presence of D-galactono-1,4-lactone. The influence on the mycelia growth was investigated by light microscopy (LM) and transmission electron microscopy (TEM) showing important alterations. © 2002 Elsevier Science Ltd. All rights reserved.

Registro:

Documento: Artículo
Título:Influence of exo β-D-galactofuranosidase inhibitors in cultures of Penicillium fellutanum and modifications in hyphal cell structure
Autor:Mariño, K.; Lima, C.; Maldonado, S.; Marino, C.; De Lederkremer, R.M.
Filiación:CIHIDECAR, Departamento De Química Orgánica, Ciudad Universitaria, Pabellón II, 1428 Buenos Aires, Argentina
Instituto De Recursos Biológicos, INTA, 1712 Castelar, Pcia. de Buenos Aires, Argentina
Palabras clave:Galactofuranose; Galactofuranosidase; Inhibitors; Penicillium fellutanum; Cell culture; Enzymes; Filtration; Glucose; Proteins; Transmission electron microscopy; Penicillium fellutanum; Carbohydrates; beta dextro galactofuranosidase inhibitor; carbon; enzyme; galactomannan; galactose; glucose; ribose; sugar; unclassified drug; article; cell structure; cell wall; controlled study; enzyme activity; enzyme synthesis; fungus culture; fungus growth; fungus hyphae; microscopy; mycelium; nonhuman; Penicillium; priority journal; protein aggregation; transmission electron microscopy; beta-Galactosidase; Cell Wall; Enzyme Inhibitors; Galactose; Glycoside Hydrolases; Hyphae; Microscopy, Electron; Penicillium; Penicillium; Penicillium fellutanum
Año:2002
Volumen:337
Número:10
Página de inicio:891
Página de fin:897
DOI: http://dx.doi.org/10.1016/S0008-6215(02)00073-3
Título revista:Carbohydrate Research
Título revista abreviado:Carbohydr. Res.
ISSN:00086215
CODEN:CRBRA
CAS:beta-Galactosidase, EC 3.2.1.23; Enzyme Inhibitors; exo-beta-D-galactofuranosidase, EC 3.2.1.-; Galactose, 26566-61-0; Glycoside Hydrolases, EC 3.2.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v337_n10_p891_Marino

Referencias:

  • Lederkremer, R.M., Colli, W., (1995) Glycobiology, 5, pp. 547-552
  • Daffe, M., Brennan, P.J., McNeil, M., (1990) J. Biol. Chem., 265, pp. 6734-6743
  • Whitfield, C., Richards, J.C., Perry, M.B., Clarke, B.R., MacLean, L.L., (1991) J. Bacteriol., 173, pp. 1420-1431
  • Lederkremer, R.M., Lima, C., Ramirez, M.I., Ferguson, M.A.J., Homans, S.W., Thomas-Oates, J., (1991) J. Biol. Chem., 266, pp. 23670-23675
  • Turco, S.J., Descoteaux, A., (1992) Annu. Rev. Microbiol., 46, pp. 65-94
  • Pan, F., Jackson, M., Ma, Y., McNeil, M., (2001) J. Bacteriol., pp. 3991-3998
  • Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F., Gander, J.E., (1977) J. Biol. Chem., 252, pp. 3219-3226
  • Daley, L.S., Strobel, G.A., (1983) Sci. Lett., 30, pp. 145-154
  • Cousin, M.A., Notermans, S., Hoogerhout, P., Van Boom, J.H., (1989) J. Appl. Bacteriol., 66, pp. 311-317
  • Köplin, R., Brisson, J.R., Whitfield, C., (1997) J. Biol. Chem., 272, pp. 4121-4128
  • Lee, R., Monsey, D., Weston, A., Duncan, K., Rithner, C., McNeil, M., (1996) Anal. Biochem., 242, pp. 1-7
  • Sanders, D.A.R., Staines, A.G., McMahon, S.A., McNeil, M.R., Whitfield, C., Naismith, J.H., (2001) Nature Struct. Biol., 8, pp. 858-863
  • Kremer, L., Dover, L.G., Morehouse, C., Hitchin, P., Everett, M., Morris, H.R., Dell, A., Besra, G.S., (2001) J. Biol. Chem., 276, pp. 26430-26440
  • Marino, C., Mariño, K., Miletti, L.C., Alves, M.J.M., Colli, W., Lederkremer, R.M., (1998) Glycobiology, 8, pp. 901-904
  • Miletti, L.C., Marino, C., Mariño, K., Lederkremer, R.M., Colli, W., Alves, M.J.M., (1999) Carbohydr. Res., 320, pp. 176-182
  • Wallis, G.L.F., Hemming, F.W., Peberdy, J.F., (2001) FEMS Microbiol. Lett., 201, pp. 21-27
  • Rick, P.D., Gander, J.E., Jentoft, N.H., Drewes, L.R., (1974) J. Biol. Chem., 249, pp. 2063-2072
  • Unkefer, C.J., Gander, J.E., (1990) J. Biol. Chem., 265, pp. 685-689
  • Gander, J.E., Laybourn, C.J., (1981) Rec. Adv. Phytochem., 15, pp. 59-91
  • Gander, J.E., Fang, F., (1974) Biochem. Biophys. Res. Commun., 58, pp. 368-374
  • Preston, J.F., Gander, J.E., (1968) Arch. Biochem., 124, pp. 504-512
  • Pletcher, C.H., Lomar, P.D., Gander, J.E., (1981) Exp. Mycol., 5, pp. 133-139
  • Birk, R., Ikan, A., Bravdo, B., Braun, S., Shoseyov, O., (1997) Appl. Biochem. Biotechnol., 66, pp. 25-30
  • Legler, G., (1990) Adv. Carbohydr. Chem. Biochem., 48, pp. 319-384
  • Ukeda, K., Hayaishi, O., (1985) Annu. Rev. Biochem., 54, pp. 73-100
  • Mitraki, A., Betton, J.-M., Desmadril, M., Yon, J., (1987) Eur. J. Biochem., 163, pp. 29-34
  • Clutterbuck, P.W., Haworth, W.N., Raistrick, H., Smith, G., Stacey, M., (1934) Biochem. J., 28, pp. 94-110
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., (1951) J. Biol. Chem., 193, pp. 265-275
  • Dubois, M., Hamilton, J., Rebers, P., Smith, F., (1956) Anal. Chem., 28, pp. 350-356
  • Segrest, J.P., Jackson, R.L., (1972) Methods Enzymol., 28, pp. 54-63
  • Korn, E.D., Wright, P.L., (1973) J. Biol. Chem., 248, pp. 439-447
  • Varela, O., Marino, C., Lederkremer, R.M., (1986) Carbohydr. Res., 155, pp. 247-251
  • Feder, R.G., O'Brien, T., (1968) Am. J. Bot., 55, pp. 123-142

Citas:

---------- APA ----------
Mariño, K., Lima, C., Maldonado, S., Marino, C. & De Lederkremer, R.M. (2002) . Influence of exo β-D-galactofuranosidase inhibitors in cultures of Penicillium fellutanum and modifications in hyphal cell structure. Carbohydrate Research, 337(10), 891-897.
http://dx.doi.org/10.1016/S0008-6215(02)00073-3
---------- CHICAGO ----------
Mariño, K., Lima, C., Maldonado, S., Marino, C., De Lederkremer, R.M. "Influence of exo β-D-galactofuranosidase inhibitors in cultures of Penicillium fellutanum and modifications in hyphal cell structure" . Carbohydrate Research 337, no. 10 (2002) : 891-897.
http://dx.doi.org/10.1016/S0008-6215(02)00073-3
---------- MLA ----------
Mariño, K., Lima, C., Maldonado, S., Marino, C., De Lederkremer, R.M. "Influence of exo β-D-galactofuranosidase inhibitors in cultures of Penicillium fellutanum and modifications in hyphal cell structure" . Carbohydrate Research, vol. 337, no. 10, 2002, pp. 891-897.
http://dx.doi.org/10.1016/S0008-6215(02)00073-3
---------- VANCOUVER ----------
Mariño, K., Lima, C., Maldonado, S., Marino, C., De Lederkremer, R.M. Influence of exo β-D-galactofuranosidase inhibitors in cultures of Penicillium fellutanum and modifications in hyphal cell structure. Carbohydr. Res. 2002;337(10):891-897.
http://dx.doi.org/10.1016/S0008-6215(02)00073-3