Pentamidine activates T1 the hepatic microsomal glucose 6-phosphate transport protein of the glucose-6-phosphatase system

1991 ◽  
Vol 1097 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Hazel M. Scott ◽  
Ann Burchell
Keyword(s):  
Phosphate Transport ◽  
Transport Protein ◽  
Phosphatase System

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.

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 Identification and characterization of a hepatic microsomal glucose transport protein. T3 of the glucose-6-phosphatase system?

1991 ◽  
Vol 275 (2) ◽  
pp. 363-367 ◽  
Author(s):  
I D Waddell ◽  
H Scott ◽  
A Grant ◽  
A Burchell
Keyword(s):  
Glucose Transport ◽  
Liver Microsomes ◽  
Inhibitory Effect ◽  
Cross Reactivity ◽  
Transport Protein ◽  
Rat Liver Microsomes ◽  
Glucose Binding ◽  
Phosphatase System ◽  
Glucose Transport Protein ◽  
Glucose Binding Protein

A 52 kDa polypeptide in rat liver microsomes was identified as a glucose-binding protein by its ability to weakly bind cytochalasin B and by its cross-reactivity to an antibody raised against the human erythrocyte glucose transport protein. The microsomal glucose binding polypeptide was purified by affinity chromatography and an antibody was raised against it. The inhibitory effect of this antibody on rat microsomal glucose-6-phosphatase activity and on glucose transport out of microsomal vesicles indicates that this protein is a microsomal glucose transport protein.

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