Pressure effect on the stability and the conformational dynamics of the D-Galactose/D-Glucose-binding protein from Escherichia coli

2005 ◽  
Vol 62 (1) ◽  
pp. 193-201 ◽  
Author(s):  
Anna Marabotti ◽  
Petr Herman ◽  
Maria Staiano ◽  
Antonio Varriale ◽  
Marcella de Champdoré ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pressure Effect ◽  
Binding Protein ◽  
Conformational Dynamics ◽  
Glucose Binding ◽  
The Stability ◽  
Glucose Binding Protein

scholarly journals D-galactose/D-glucose-binding Protein from Escherichia coli as Probe for a Non-consuming Glucose Implantable Fluorescence Biosensor

Sensors ◽  
2007 ◽  
Vol 7 (10) ◽  
pp. 2484-2491 ◽  
Author(s):  
Viviana Scognamiglio ◽  
Vincenzo Aurilia ◽  
Nunzio Cennamo ◽  
Paola Ringhieri ◽  
Luisa Iozzino ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Glucose Binding ◽  
Fluorescence Biosensor ◽  
Glucose Binding Protein

scholarly journals Structure and stability of D-galactose/D-glucose-binding protein. The role of D-glucose binding and Ca ion depletion

2010 ◽  
Vol 24 (3-4) ◽  
pp. 355-359 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Olga I. Povarova ◽  
Olesya V. Stepanenko ◽  
Alexander V. Fonin ◽  
Irina M. Kuznetsova ◽  
...  
Keyword(s):  
Protein Unfolding ◽  
Binding Protein ◽  
Guanidine Hydrochloride ◽  
Protein Fluorescence ◽  
Structure And Stability ◽  
Glucose Binding ◽  
One Step ◽  
The Stability ◽  
Glucose Binding Protein

The effects of guanidine hydrochloride (GdnHCl) on the structure and stability of the D-galactose/D-glucose-binding protein fromEscherichia coli(GGBP) and its complex with D-glucose (GGBP/Glc) were investigated by intrinsic protein fluorescence and far-UV circular dichroism (CD). The role of calcium in the stability of the protein structure was also studied. It was shown that the processes of GGBP and GGBP/Glc unfolding induced by GdnHCl followed one-step reversible denaturation mechanism. The obtained data showed that the binding of glucose to GGBP resulted in an increase of the protein stability towards the actions of the GdnHCl which made protein unfolding more cooperative. The stabilities of GGBP alone, GGBP in the presence of glucose, GGBP-depleted calcium (GGBP-Ca), and GGBP/Glc-depleted calcium (GGBP/Glc-Ca) were characterized by difference of Gibbs free energies.

Labeling of a glucose binding protein in the rabbit intestinal brush border membrane

1978 ◽  
Vol 56 (5) ◽  
pp. 760-770 ◽  
Author(s):  
J. Lemaire ◽  
D. Maestracci
Keyword(s):  
Molecular Weight ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Binding Protein ◽  
Electrophoretic Pattern ◽  
Protein Band ◽  
Relative Mobility ◽  
Intestinal Brush Border ◽  
Glucose Binding ◽  
Glucose Binding Protein

Using a double labeling method based on the method of Thomas (Thomas, L. 1973. Isolation of N-ethylmaleimide-labeled phloridzin-sensitive D-glucose binding protein of brash border membrane from rat kidney cortex. Biochim. Biophys. Acta, 291, 454–464.), with radioactive N-ethylmaleimide ([3H]NEM and [14C]NEM) in the presence and absence of D-glucose, a protein band which is periodic acid – Schiff staining insensitive and which has a relative mobility (Rm) of 0.55 (corresponding to a molecular weight of 51 000 daltons) as determined by sodium dodecyl sulfate (SDS) electrophoresis was labeled preferentially.When radioactive p-hydroxymercuriphenylsulfonate ([203Hg]PCMBS) is used in the presence and absence of D-glucose, as described by Smith et al. (SMITH, M. W., FERGUSON, D. R., and BURTON, K. A. 1975. Glucose- and phloridzin-protected thiol groups in pig intestinal brush border membranes. Biochern. J. 147, 617–619.), a protein band which has a relative mobility of 0.62 and a corresponding molecular weight of 42 000 daltons was labeled.Control experiments have shown that increasing concentrations of nonradioactive NEM (0.1–5.0 mM) do not substantially modify the electrophoretic pattern of SDS-solubilized brush border membrane. Nonradioactive PCMBS (0.1–10 mM), on the other hand, modifies the electrophoretic pattern and especially causes a change in relative mobility of the 0.55 protein band which migrates after 1 mM PCMBS treatment with a Rm of 0.62.The effect of 1 mM PCMBS can be reversed by adding L-cysteine or dithiotreitol.Actin extracted from rabbit muscle migrates with the same Rm as the 0.55 protein band in our electrophoretic conditions.

Preformulation Characterization, Stabilization, and Formulation Design for the Acrylodan-Labeled Glucose-Binding Protein SM4-AC

2017 ◽  
Vol 106 (5) ◽  
pp. 1197-1210 ◽  
Author(s):  
Neha Sahni ◽  
Rajoshi Chaudhuri ◽  
John M. Hickey ◽  
Prakash Manikwar ◽  
Ajit D’Souza ◽  
...  
Keyword(s):  
Binding Protein ◽  
Formulation Design ◽  
Glucose Binding ◽  
Glucose Binding Protein

Substrate specificity of the high-affinity glucose transport system of Pseudomonas aeruginosa

1993 ◽  
Vol 39 (7) ◽  
pp. 722-725 ◽  
Author(s):  
John L. Wylie ◽  
Elizabeth A. Worobec
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Glucose Transport ◽  
Transport System ◽  
Binding Protein ◽  
High Affinity ◽  
Glucose Binding ◽  
Glucose Transport System ◽  
Glucose Binding Protein

Specificity of the high-affinity glucose transport system of Pseudomonas aeruginosa was examined. At a concentration of [14C]glucose near the Vmax of the system, inhibition by maltose, galactose, and xylose was detected. This inhibition is similar to that detected in earlier in vivo studies and correlates with the known specificity of OprB, a glucose-specific porin of P. aeruginosa. At a level of [14C]glucose 100 times lower, only unlabelled glucose inhibited uptake to any extent. This matches the known in vitro specificity of the periplasmic glucose binding protein. These findings were used to explain the discrepancy between earlier in vivo and in vitro results reported in the literature.Key words: Pseudomonas aeruginosa, glucose transport, OprB, glucose binding protein.

scholarly journals Single-stranded DNA-binding protein enhances the stability of CTG triplet repeats in Escherichia coli.

1996 ◽  
Vol 178 (16) ◽  
pp. 5042-5044 ◽  
Author(s):  
W A Rosche ◽  
A Jaworski ◽  
S Kang ◽  
S F Kramer ◽  
J E Larson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Triplet Repeats ◽  
Single Stranded Dna ◽  
The Stability
Sign in / Sign up

Export Citation Format

Share Document