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Titolo:
ISOLATION, PURIFICATION, AND CHARACTERIZATION OF DMSP LYASE (DIMETHYLPROPIOTHETIN-DETHIOMETHYLASE-(4.4.1.3)) FROM THE RED ALGA POLYSIPHONIA-PANICULATA
Autore:
NISHIGUCHI MK; GOFF LJ;
Indirizzi:
UNIV SO CALIF,DEPT BIOL SCI,UNIV PK LOS ANGELES CA 90089 UNIV CALIF SANTA CRUZ,DEPT BIOL SANTA CRUZ CA 00000
Titolo Testata:
Journal of phycology
fascicolo: 4, volume: 31, anno: 1995,
pagine: 567 - 574
SICI:
0022-3646(1995)31:4<567:IPACOD>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
TETRASELMIS-SUBCORDIFORMIS STEIN; LANOSA L TANDY; BETA-DIMETHYLSULPHONIOPROPIONATE; ENHANCED PROTECTION; DIMETHYL SULFIDE; DIVALENT-CATIONS; GREEN MACROALGAE; ESTUARINE SITES; MARINE; DIMETHYLSULFONIOPROPIONATE;
Keywords:
DIMETHYLSULFONIOPROPIONATE; DIMETHYLSULFIDE; DMSP LYASE; OSMOLYTE; OSMOREGULATION; SOLUTE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
M.K. Nishiguchi e L.J. Goff, "ISOLATION, PURIFICATION, AND CHARACTERIZATION OF DMSP LYASE (DIMETHYLPROPIOTHETIN-DETHIOMETHYLASE-(4.4.1.3)) FROM THE RED ALGA POLYSIPHONIA-PANICULATA", Journal of phycology, 31(4), 1995, pp. 567-574

Abstract

Polysiphonia paniculata Montagne is an intertidal red alga known to produce large amounts of the compound dimethylsulfoniopropionate (DMSP). Conversion of this substrate into dimethylsulfide is accomplished inP. paniculata by an enzyme called DMSP lyase (dimethylpropiothetin dethiomethylase (4. 4. 1.3)). DMSP lyase has been purified and characterized from P. paniculata. Enzyme activity is found in two different proteins: the larger with a molecular weight of 9.26 x 10(4) daltons and the smaller with a molecular weight of 3.65 x 10(4) daltons. Specific activity of the enzyme is 526 mu mols . min(-1). mg(-1) for the smaller protein and 263 mu mols . min(-1). mg(-1) for the larger protein. The Michaelis-Menten constant (K-m) is 72.8 mu M +/- 17.15 and the nu(max) is 1.62 mu mols . min(-1) +/- 0.928 for the 92. 6-kDa protein. The pi of the larger protein is 5.8 and 5.9 for the smaller protein. Interaction with cysteine protease inhibitors L-trans-epoxysuccinyl-leucylamido (4-guanidino)-butane, dithiobis-(2-nitrobenzoate), or N-ethylmaleimide inactivated enzyme activity. The presence of either magnesium orcalcium with DMSP lyase enhanced activity at concentrations between 20 and 40 mu M but had little effect above these bevels. Addition of the divalent chelators ethylenebis(oxyethylenenitrilo) tetracetic acid and ethtlenediaminetetraacetate decreased activity of the enzyme, but activity was restored when either chelator was removed and magnesium orcalcium was added to the enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:53:02