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Titolo:
F-19 NMR MEASUREMENTS OF THE ROTATIONAL MOBILITY OF PROTEINS IN-VIVO
Autore:
WILLIAMS SP; HAGGLE PM; BRINDLE KM;
Indirizzi:
UNIV CAMBRIDGE,DEPT BIOCHEM,TENNIS COURT RD CAMBRIDGE CB2 1QW ENGLAND UNIV CAMBRIDGE,DEPT BIOCHEM CAMBRIDGE CB2 1QW ENGLAND
Titolo Testata:
Biophysical journal
fascicolo: 1, volume: 72, anno: 1997,
pagine: 490 - 498
SICI:
0006-3495(1997)72:1<490:FNMOTR>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST PHOSPHOGLYCERATE KINASE; NUCLEAR MAGNETIC-RESONANCE; ENZYME-ENZYME INTERACTIONS; D-LACTATE DEHYDROGENASE; LIVING 3T3 CELLS; PYRUVATE-KINASE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; SACCHAROMYCES-CEREVISIAE; QUANTITATIVE-EVALUATION; DIFFUSION-COEFFICIENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
84
Recensione:
Indirizzi per estratti:
Citazione:
S.P. Williams et al., "F-19 NMR MEASUREMENTS OF THE ROTATIONAL MOBILITY OF PROTEINS IN-VIVO", Biophysical journal, 72(1), 1997, pp. 490-498

Abstract

Three glycolytic enzymes, hexokinase, phosphoglycerate kinase, and pyruvate kinase, were fluorine labeled in the yeast Saccharomyces cerevisiae by biosynthetic incorporation of 5-fluorotryptophan, F-19 NMR longitudinal relaxation time measurements on the labeled enzymes were used to assess their rotational mobility in the intact cell. Comparison with the results obtained from relaxation time measurements of the purified enzymes in vitro and from theoretical calculations showed that two of the labeled enzymes, phosphoglycerate kinase and hexokinase, weretumbling in a cytoplasm that had a viscosity approximately twice thatof water. There were no detectable signals from pyruvate kinase in vivo, although it could be detected in diluted cell extracts, indicatingthat there was some degree of motional restriction of the enzyme in the intact cell.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 20:31:57