A Strategic Fluorescence Labeling ofd-Galactose/d-Glucose-Binding Protein fromEscherichiacoliHelps to Shed Light on the Protein Structural Stability and Dynamics

2007 ◽  
Vol 6 (11) ◽  
pp. 4119-4126 ◽  
Author(s):  
Viviana Scognamiglio ◽  
Andrea Scirè ◽  
Vincenzo Aurilia ◽  
Maria Staiano ◽  
Roberta Crescenzo ◽  
...  
Keyword(s):  
Structural Stability ◽  
Binding Protein ◽  
Fluorescence Labeling ◽  
Glucose Binding ◽  
Glucose Binding Protein ◽  
Shed Light

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.

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

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 Structure of a periplasmic glucose-binding protein fromThermotoga maritima

2012 ◽  
Vol 68 (12) ◽  
pp. 1460-1464 ◽  
Author(s):  
Kandavelu Palani ◽  
Desigan Kumaran ◽  
Stephen K. Burley ◽  
Subramanyam Swaminathan
Keyword(s):  
Binding Protein ◽  
Glucose Binding ◽  
Glucose Binding Protein

scholarly journals Fluorophore-labeled bioengineered glucose binding protein for measurement of transdermal glucose

2016 ◽  
Vol 64 ◽  
pp. 25-32
Author(s):  
Cristina Tiangco ◽  
Sheniqua Brown ◽  
Fortunato Sevilla III ◽  
Govind Rao ◽  
Leah Tolosa
Keyword(s):  
Binding Protein ◽  
Glucose Binding ◽  
Glucose Binding Protein
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