Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Nucleotide-binding sites in the functional unit of sarcoplasmic reticulum Ca2+-ATPase as studied by photoaffinity spin-labeled 2-N-3-SL-ATP
Autore:
Palm, T; Coan, C; Trommer, WE;
Indirizzi:
Univ Kaiserslautern, Fachbereich Chem, D-67663 Kaiserslautern, Germany Univ Kaiserslautern Kaiserslautern Germany D-67663 iserslautern, Germany Univ Pacific, Sch Dent, Dept Physiol, San Francisco, CA 94115 USA Univ Pacific San Francisco CA USA 94115 siol, San Francisco, CA 94115 USA
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 382, anno: 2001,
pagine: 417 - 423
SICI:
1431-6730(200103)382:3<417:NSITFU>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-PARAMAGNETIC-RES; CA-ATPASE; ENZYME-KINETICS; CALCIUM-PUMP; PROTEIN; MECHANISM; PHOSPHORYLATION; STOICHIOMETRY; ORIENTATION; SUBSTRATE;
Keywords:
Ca2+-ATPase; ESR-spectroscopy; photoaffinity-label; reconstitution; sarcoplasmic; reticulum; spin-label;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Trommer, WE Univ Kaiserslautern, Fachbereich Chem, Erwin Schrodinger Str, D-67663 Kaiserslautern, Germany Univ Kaiserslautern Erwin Schrodinger Str Kaiserslautern Germany D-67663
Citazione:
T. Palm et al., "Nucleotide-binding sites in the functional unit of sarcoplasmic reticulum Ca2+-ATPase as studied by photoaffinity spin-labeled 2-N-3-SL-ATP", BIOL CHEM, 382(3), 2001, pp. 417-423

Abstract

2-N-3-SL-ATP [2-azido-2 ' ,3 ' -0-(1-oxyl-2,2,5,5-tetram-ethyl-3-carbonyl-pyrroline) adenosine triphosphate], a photoaffinity spin-labeled derivativeof AIP with a nitroxide moiety attached to the ribose ring and an azido group attached to C2 of the adenine ring, was used to study the nucleotide-binding site stoichiometry of sarcoplasmic reticulum (SR) Ca2+-AT-Pase. The label was shown to bind at the catalytic site of the enzyme, even though therate of hydrolysis was poor. A maximal binding ratio of 1 mol/mol of ATPase was found. The ESR spectra showed signals from spin-spin interactions between two radicals corresponding to a distance of about 15 Angstrom between labels bound to adjacent sites on the enzyme. This indicates that the minimal functional unit of the Ca2+-ATPase is a dimer with the nucleotide-binding sites in close proximity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 07:17:45