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Titolo:
Stereospecific binding of MRI contrast agents to human serum albumin: The ease of Gd-(S)-EOB DTPA (Eovist) and its (R) isomer
Autore:
Elst, LV; Chapelle, F; Laurent, S; Muller, RN;
Indirizzi:
Univ Mons, Dept Organ Chem, NMR Lab, B-7000 Mons, Belgium Univ Mons MonsBelgium B-7000 Organ Chem, NMR Lab, B-7000 Mons, Belgium
Titolo Testata:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
fascicolo: 2, volume: 6, anno: 2001,
pagine: 196 - 200
SICI:
0949-8257(200102)6:2<196:SBOMCA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
NMR RELAXOMETRIC INVESTIGATIONS; MAGNETIC-RESONANCE ANGIOGRAPHY; GD-EOB-DTPA; PRECLINICAL EVALUATION; MS-325; COMPLEXES; WATER; RELAXATION; DIFFUSION; PROTEIN;
Keywords:
Gd-EOB-DTPA; MRI contrast agent; non-covalent binding; human serum albumin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Muller, RN Univ Mons, Dept Organ Chem, NMR Lab, B-7000 Mons, Belgium Univ Mons Mons Belgium B-7000 , NMR Lab, B-7000 Mons, Belgium
Citazione:
L.V. Elst et al., "Stereospecific binding of MRI contrast agents to human serum albumin: The ease of Gd-(S)-EOB DTPA (Eovist) and its (R) isomer", J BIOL I CH, 6(2), 2001, pp. 196-200

Abstract

The water proton relaxation rate enhancement of the hepatospecific Gd-(S)-EOB-DTPA (Eovist) and of its (R) isomer in aqueous solutions free of protein, in serum and in 4% human serum albumin solution, are compared. In the absence of proteins, both compounds exhibit, as expected, the same proton relaxivity, as measured by the nuclear magnetic relaxation dispersion (NMRD) profiles. In serum and albumin solution, non-covalent binding of the paramagnetic complexes to macromolecules is observed. Both isomers are likely to bind to the same site of human serum albumin, but the affinity of the (S) isomer is larger than for the (R) isomer.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 13:18:32