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Titolo:
Effect of glycerol on the interactions and solubility of bovine pancreatictrypsin inhibitor
Autore:
Farnum, M; Zukoski, C;
Indirizzi:
Univ Illinois, Dept Chem Engn, Roger Adams Lab 114, Urbana, IL 61801 USA Univ Illinois Urbana IL USA 61801 ger Adams Lab 114, Urbana, IL 61801 USA
Titolo Testata:
BIOPHYSICAL JOURNAL
fascicolo: 5, volume: 76, anno: 1999,
pagine: 2716 - 2726
SICI:
0006-3495(199905)76:5<2716:EOGOTI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYNAMIC LIGHT-SCATTERING; LYSOZYME SOLUTIONS; CONCENTRATION-DEPENDENCE; PROTEIN CRYSTALLIZATION; MOLECULAR-INTERACTIONS; DIFFUSION-COEFFICIENT; COLLOIDAL PARTICLES; CRYSTAL-GROWTH; BPTI MOLECULES; PHASE-BEHAVIOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Zukoski, C Univve,linois, Dept Chem Engn, Roger Adams Lab 114, Box C-3,600S Mathews A Univ Illinois Box C-3,600 S Mathews Ave Urbana IL USA 61801 s A
Citazione:
M. Farnum e C. Zukoski, "Effect of glycerol on the interactions and solubility of bovine pancreatictrypsin inhibitor", BIOPHYS J, 76(5), 1999, pp. 2716-2726

Abstract

The effects of additives used to stabilize protein structure during crystallization on protein solution phase behavior are poorly understood. Here weinvestigate the effect of glycerol and ionic strength on the solubility and strength of interactions of the bovine pancreatic trypsin inhibitor. These two variables are found to have opposite effects on the intermolecular forces; attractions increase with [NaCl], whereas repulsions increase with glycerol concentration. These changes are mirrored in bovine pancreatic trypsin inhibitor solubility where the typical salting out behavior for NaCl is observed with higher solubility found in buffers containing glycerol. The increased repulsions induced by glycerol can be explained by a number of possible mechanisms, all of which require small changes in the protein or the solvent in its immediate vicinity. Bovine pancreatic trypsin inhibitor follows the same general phase behavior as other globular macromolecules where a robust correlation between protein solution second virial coefficient andsolubility has been developed. This study extends previous reports of thiscorrelation to solution conditions involving nonelectrolyte additives.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 01:25:33