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Titolo:
PURIFICATION OF THE D-LACTATE DEHYDROGENASE FROM LEUCONOSTOC-MESENTEROIDES SSP CREMORIS USING A SEQUENTIAL PRECIPITATION PROCEDURE
Autore:
SHU HC; DONG GQ; KAUL R; MATTIASSON B;
Indirizzi:
LUND UNIV,CTR CHEM,DEPT BIOTECHNOL S-22100 LUND SWEDEN LUND UNIV,CTR CHEM,DEPT BIOTECHNOL S-22100 LUND SWEDEN
Titolo Testata:
Journal of biotechnology
fascicolo: 1, volume: 34, anno: 1994,
pagine: 1 - 11
SICI:
0168-1656(1994)34:1<1:POTDDF>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
AFFINITY PRECIPITATION; PROTEINS; DYES;
Keywords:
D-LACTATE DEHYDROGENASE; PURIFICATION; LEUCONOSTOC MESENTEROIDES; SELECTIVE PRECIPITATION; EUDRAGIT, MODIFIED; CIBACRON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
H.C. Shu et al., "PURIFICATION OF THE D-LACTATE DEHYDROGENASE FROM LEUCONOSTOC-MESENTEROIDES SSP CREMORIS USING A SEQUENTIAL PRECIPITATION PROCEDURE", Journal of biotechnology, 34(1), 1994, pp. 1-11

Abstract

Selective precipitation was used for the purification of D-lactate dehydrogenase from cell homogenate of Leuconostoc mesenteroides ssp. cremoris. This was facilitated by the use of a copolymer of methacrylic acid and methylmethacrylate with the tradename of Eudragit S 100, whichis precipitated by a pH-shift towards acidic conditions. Eudragit modified with ethanolamine was used to precipitate contaminating proteinswhich were removed along with cell debris. D-LDH was recovered from the supernatant by adsorption to Eudragit-Cibacron blue. The dissociation of the specifically bound protein was carried out by treatment withsalt. The enzyme was finally subjected to ion exchange chromatography. The enzyme was purified more than 33 times and the specific activityof the pure enzyme after the three-step process was 534 units per mg protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 20:37:05