Purified mitochondrial phosphate-transport protein. Improved proteoliposomes and some properties of the transport protein sulfhydryl group(s)

Biochemistry ◽  
1984 ◽  
Vol 23 (6) ◽  
pp. 1057-1064 ◽  
Author(s):  
Hartmut Wohlrab ◽  
Anne Collins ◽  
Diane Costello ◽  
Kinichi Tsunoda
Keyword(s):  
Sulfhydryl Group ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Protein Sulfhydryl

High specificity of a phosphate transport protein determined by hydrogen bonds

Nature ◽  
1990 ◽  
Vol 347 (6291) ◽  
pp. 402-406 ◽  
Author(s):  
Hartmut Luecke ◽  
Florante A. Quiocho
Keyword(s):  
Hydrogen Bonds ◽  
High Specificity ◽  
Phosphate Transport ◽  
Transport Protein

scholarly journals Protein Sulfhydryl Group Oxidation and Mixed-Disulfide Modifications in Stable and Unstable Human Carotid Plaques

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Antonio Junior Lepedda ◽  
Angelo Zinellu ◽  
Gabriele Nieddu ◽  
Elisabetta Zinellu ◽  
Ciriaco Carru ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Function ◽  
Sulfhydryl Group ◽  
Plaque Stability ◽  
Proteomic Approach ◽  
Oxidative Modifications ◽  
Protein Sulfhydryl ◽  
Unstable Plaques ◽  
Protein Sulfhydryl Groups ◽  
Human Carotid

Objectives. Oxidative stress has been implicated in the outcome of atherosclerotic plaques. However, at present, no data are available neither on the degree of plaque protein sulfhydryl groups oxidation nor on its relationship with plaque vulnerability. We investigated the entity of protein-SH oxidative modifications, focusing on low molecular weight thiols adduction, in human carotid plaque extracts in relation to plaque stability/instability.Methods. Plaque stability/instability was histologically assessed. The extent of protein-SH oxidative modifications was established by a differential proteomic approach on fluorescein-5-maleimide-labeled plaque extracts and corresponding plasma samples from 48 endarterectomized patients. The analysis on protein thiolation was performed by capillary zone electrophoresis.Results. We observed a higher protein-SH oxidation of both plasma-derived and topically expressed proteins in unstable plaques, partly due to higher levels of S-thiolation. Conversely, in plasma, none of the investigated parameters discriminated among patients with stable and unstable plaques.Conclusions. Our results suggest the presence of a more pronounced oxidative environment in unstable plaques. Identifying specific oxidative modifications and understanding their effects on protein function could provide further insight into the relevance of oxidative stress in atherosclerosis.

scholarly journals Analysis of human hepatic microsomal glucose-6-phosphatase in clinical conditions where the T2 pyrophosphate/phosphate transport protein is absent

1992 ◽  
Vol 281 (3) ◽  
pp. 859-863 ◽  
Author(s):  
R C Nordlie ◽  
H M Scott ◽  
I D Waddell ◽  
R Hume ◽  
A Burchell
Keyword(s):  
Endoplasmic Reticulum ◽  
Transport System ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Hepatic Microsomes ◽  
Phosphatase System ◽  
Pyrophosphatase Activity ◽  
Protein Components ◽  
Clinical Conditions

The availability of a rare set of human hepatic microsomes in which T2, a pyrophosphate/phosphate transport protein of the glucose-6-phosphatase system, has been shown immunologically to be completely absent, has permitted further characterization of multicomponent glucose-6-phosphatase (EC 3.1.3.9). Pyrophosphatase activity in intact microsomes was found to be totally absent, but was normal in disrupted microsomes. However, Pi did not accumulate within the lumen of the microsomes when glucose 6-phosphate was the substrate. This was not as predicted if there is only one transport protein in the endoplasmic reticulum capable of transporting Pi, produced by glucose-6-phosphatase, out of the lumen. The results suggest that the pyrophosphate/phosphate transport system of human hepatic endoplasmic reticulum must be more complex than previously thought, as it must comprise at least two protein components.

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