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Titolo:
Comparison of solubility and interactions of aprotinin (BPTI) solutions inH2O and D2O
Autore:
Budayova-Spano, M; Lafont, S; Astier, JP; Ebel, C; Veesler, S;
Indirizzi:
CNRS, CRMC3, Ctr Rech Mecanismes Croissance Cristalline, F-13288 Marseille09, France CNRS Marseille France 09 ssance Cristalline, F-13288 Marseille09, France UJF, Inst Biol Struct JP Ebel, Mol Biophys Lab, CNRS,CEA,UMR 5075, F-38027Grenoble, France UJF Grenoble France F-38027 , CNRS,CEA,UMR 5075, F-38027Grenoble, France
Titolo Testata:
JOURNAL OF CRYSTAL GROWTH
fascicolo: 3, volume: 217, anno: 2000,
pagine: 311 - 319
SICI:
0022-0248(200008)217:3<311:COSAIO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXPONENTIAL-SAMPLING METHOD; DYNAMIC LIGHT-SCATTERING; DILATIONALLY INVARIANT TRANSFORMS; PANCREATIC ALPHA-AMYLASE; AMINO-ACID-SEQUENCE; CORRELATION SPECTROSCOPY; PROTEIN CRYSTALLIZATION; LYSOZYME SOLUBILITY; CRYSTAL-GROWTH; POLYDISPERSITY;
Keywords:
BPTI; H2O/D2O; solubility; molecules association; interactions;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
--discip_EC--
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Veesler, S CNRS, CRMC3, Ctr Rech Mecanismes Croissance Cristalline, CampusLuminy,Case 913, F-13288 Marseille 09, France CNRS Campus Luminy,Case 913 Marseille France 09 lle 09, France
Citazione:
M. Budayova-Spano et al., "Comparison of solubility and interactions of aprotinin (BPTI) solutions inH2O and D2O", J CRYST GR, 217(3), 2000, pp. 311-319

Abstract

Small-angle neutron scattering experiments are often performed with proteins solubilized in heavy water because of the large difference in neutron scattering properties of protons and deuterons. In order to characterize the effect of D2O on physico-chemical properties of protein solutions, we investigated the effect of D2O on the phase diagram and the interactions of bovine pancreatic trypsin inhibitor (BPTI) in solution. We measured the solubility in D2O of BPTI solutions in the presence of NaCl (reverse solubility) and KSCN (direct solubility) and compared with the values measured by Lafontet al. in H2O under the same conditions [Lafont et al., J. Crystal Growth 173 (1997) 132]. In the two salts, we found that BPTI solubility in D2O is significantly lower than in H2O. The curves representing the solubility of BPTI in KSCN are shifted by 7.2 degrees C between light and heavy water, a shift obtained previously with lysozyme and representing the difference in the temperature of maximum density of both types of water [Gripon et al., J. Crystal Growth 177 (1997) 238; 178 (1997) 575]. In the case of BPTI in NaCl, we did not find this relationship between the solubility in H2O and D2O. We found, by dynamic light scattering, that BPTI attractive intermolecular interactions in the presence of NaCl in D2O are significantly stronger than in H2O. We investigated the association of BPTI molecules in crystallization conditions in the presence of NaCl in H2O and D2O by small-angle X-rayand neutrons scattering, respectively. In the presence of heavy water, thetransition monomer-multimer is observed at about 2 mg/ml of BPTI in 1 M NaCl whereas in light water and in 1.4 M NaCl solution this transition is observed at about 15 mg/ml. These results dearly showed that BPTI in crystallization conditions is a multimer and confirm the importance of the isotopic nature of water in the crystallization of proteins. The replacement of H2O by D2O decreases the solubility and increases the attractive intermolecularinteractions. (C) 2000 Elsevier Science B.V. All rights reserved.

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Documento generato il 13/07/20 alle ore 11:07:20