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Effect of pH and buffers on insulin binding to normal and neoplastic mammary cells, fat cells and membrane preparations.
Metadata
JournalCancer Biochem. Biophys.Not FoundDate
1979
Type
Research Support, U.S. Gov't, P.H.S.
Research Support, Non-U.S. Gov't
Journal Article
Comparative Study
Volume
1979 / 4 : 51-7
Author
Shafie SM , Cech JM , Livingston JN , Hilf R
Doi
Not Found
PMIDMESH
Adenocarcinoma
Adipose Tissue
Animals
Biological Transport, Active
Cell Membrane
Female
Glucose
Hydrogen-Ion Concentration
Insulin
Kinetics
Mammary Glands, Animal
Mammary Neoplasms, Experimental
Rats
Receptor, Insulin
Abstract
As a function of buffer pH, [125I]-insulin binding to rat mammary cells, rat adipocytes, or membranes prepared therefrom, at 4 degrees or 20 degrees C, showed 2 peaks in different buffers. Specific insulin binding at the pH 7.7. peak (100 +/- 11%) was lower than at pH 8.8 (140 +/- 17%) with no change in nonspecific binding. Although insulin stimulation of glucose uptake into fat cells was highest at pH 7.5, this response was also seen at pH 8.6. Scatchard affinity profiles, or in the kinetics of dissociation. Insulin degradation (< 10%) and binding to insulin antibody were similar over the pH range of 7 to 9.
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Cancer Biochem. Biophys.Cancer biochemistry biophysics
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