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Titolo:
PURIFICATION AND FUNCTIONAL RECONSTITUTION OF THE 2-OXOGLUTARATE MALATE TRANSLOCATOR FROM SPINACH-CHLOROPLASTS
Autore:
MENZLAFF E; FLUGGE UI;
Indirizzi:
UNIV WURZBURG,JULIUS VON SACHS INST BIOWISSENSCH,LEHRSTUHL BOT 1 W-8700 WURZBURG GERMANY UNIV WURZBURG,JULIUS VON SACHS INST BIOWISSENSCH,LEHRSTUHL BOT 1 W-8700 WURZBURG GERMANY
Titolo Testata:
Biochimica et biophysica acta
fascicolo: 1, volume: 1147, anno: 1993,
pagine: 13 - 18
SICI:
0006-3002(1993)1147:1<13:PAFROT>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATE TRANSLOCATOR; INNER MEMBRANE; DICARBOXYLATE TRANSPORT; CARRIER PROTEIN; ENVELOPE; AMMONIA; STIMULATION; EVOLUTION; GLUTAMATE; SEQUENCE;
Keywords:
2-OXOGLUTARATE MALATE TRANSLOCATOR; CHLOROPLAST; DICARBOXYLATE TRANSPORT; RECONSTITUTION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
E. Menzlaff e U.I. Flugge, "PURIFICATION AND FUNCTIONAL RECONSTITUTION OF THE 2-OXOGLUTARATE MALATE TRANSLOCATOR FROM SPINACH-CHLOROPLASTS", Biochimica et biophysica acta, 1147(1), 1993, pp. 13-18

Abstract

The chloroplast 2-oxoglutarate/malate translocator was solubilized from envelope membranes by the detergent n-dodecyl beta-D-maltoside and purified to apparent homogeneity by anion-exchange chromatography followed by gel permeation chromatography. During the purification procedure, the activity of the translocator was monitored by functional reconstitution into phospholipid vesicles. The purified translocator protein has an apparent molecular mass of about 45 000 as revealed by SDS-PAGE. Based on the specific reconstituted transport activity, the purification was about 31-fold with an overall yield of congruent-to 50%. The substrate specificity of the purified translocator closely resemblesthat described for the native transport system in intact chloroplasts.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:23:48