SUPREX (Stability of Unpurified Proteins from Rates of H/D Exchange) Analysis of the Thermodynamics of Synergistic Anion Binding by Ferric-Binding Protein (FbpA), a Bacterial Transferrin†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15767-15774 ◽  
Author(s):  
Petra L. Roulhac ◽  
Kendall D. Powell ◽  
Suraj Dhungana ◽  
Katherine D. Weaver ◽  
Timothy A. Mietzner ◽  
...  
2003 ◽  
Vol 100 (7) ◽  
pp. 3659-3664 ◽  
Author(s):  
S. Dhungana ◽  
C. H. Taboy ◽  
D. S. Anderson ◽  
K. G. Vaughan ◽  
P. Aisen ◽  
...  

2005 ◽  
Vol 280 (10) ◽  
pp. 9283-9290 ◽  
Author(s):  
Stacey A.L. Tom-Yew ◽  
Diana T. Cui ◽  
Elena G. Bekker ◽  
Michael E.P. Murphy

PEDIATRICS ◽  
1971 ◽  
Vol 47 (5) ◽  
pp. 811-817
Author(s):  
Gerhard Levy ◽  
Inta J. Ertel

The formation of glucuronides of salicylate, salicylamide, and acetaminophen in two sisters with congenital unconjugated hyperbilirubinemia responsive to phenobarbital was normal at widely different (6 to 37 mg per 100 ml) serum bilirubin concentrations. The conjugation of salicylate with glycine, and the formation of salicylamide sulfate and acetaminophen sulfate were also normal. This shows that unconjugated hyperbilirubinemia per se does not affect the biotransformation of the three drugs tested. The clinical and pharmacokinetic characteristics of the children in this study are consistent with a recently proposed mechanism involving a deficiency in hepatic anion-binding protein (rather than glucuronyl transferase) as one cause of unconjugated hyperbilirubinemia.


1997 ◽  
Vol 25 (5) ◽  
pp. 979-987 ◽  
Author(s):  
Shane D. Kirby ◽  
Scott D. Gray‐Owen ◽  
Anthony B. Schryvers

1975 ◽  
Vol 55 (5) ◽  
pp. 1009-1019 ◽  
Author(s):  
R Kirsch ◽  
G Fleischner ◽  
K Kamisaka ◽  
I M Arias

2018 ◽  
Author(s):  
Matt Bawn ◽  
Justin Bradley ◽  
Fraser MacMillan

AbstractDistance determination in proteins and biomolecules using pulsed EPR (electron paramagnetic resonance) techniques is becoming an increasingly popular and accessible technique. PELDOR (pulsed electron-electron double resonance), is a technique designed for distance determination over a nanoscopic scale. Here, ferric binding protein (Fbp) is used to demonstrate the practicability of this technique to Cu (II) Metalloproteins. PELDOR is usually applied to bi-radicals or endogenous radicals, and distance determination using pulsed EPR of metal containing centres in biomolecules has been restricted to relaxation experiments. PELDOR distance measurements between a Cu (II) ion and a nitroxide have previously only been reported for model compounds [1, 2].Fbp as the name suggests usually, contains a Fe (III) ion centre. For the purposes of this investigation the Fe (III) ion was removed and replaced by a Cu (II) ion, after a nitroxide spin-label was added to the Fbp using of site directed spin-labelling (SDSL). PELDOR was then applied to measure the distance between the two centres.Simulation methods were then employed to fully investigate these data and allow a quantitative interpretation of the copper nitroxide PELDOR data. The observed PELDOR time traces were analysed using DEER analysis[3].


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