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The endocytosis of 125I-EGF was studied in transfectant NIH3T3 cells expressing a normal full-length EGF receptor (HER14) and a mutant receptor lacking 4 major autophosphorylation sites by deletion of 126 amino acids from the carboxyl terminus (CD126). The rates of 125I-EGF internalization and degradation in CD 126 were found to be slightly lower compared(More)
To assess the functional activity of internalized epidermal growth factor (EGF) receptors in A-431 cells we investigated their ability to be both the target and activator of serine and threonine protein kinases. By incubating A-431 cells with EGF at 4 degrees C wr at 37 degrees C, eluting surface-bound EGF with an acid buffer, and immunoprecipitating the(More)
Phosphorylation of the epidermal growth factor (EGF) receptors in endosomes isolated from A431 cells was studied using antiphosphotyrosin antibody (anti-P-Tyr). A431 cells were preincubated with EGF and then washed with acid buffer to remove surface-bound EGF. Endosomes were isolated from such cells by the method of subcellular fractionation on Percoll(More)
Using cultured A431 cells, a comparative analysis was performed of endocytosis stimulated by the epidermal growth factor (EGF) just following the ligand influence (early endocytosis) and after a 3 hour incubation of A431 cells with EGF (delay endocytosis). It is shown that at the early endocytosis the total amount of 125I-EGF, associated with cells, is(More)
The ratio of tyrosine-phosphorylated EGF-receptors was estimated for surface and endosomal EGF-receptor complexes on A431 cells. The cells were incubated with 125I-EGF, and then 125I-EGF was covalently bound to the receptor by cross-linking reagent-suberate. Following the cell lysis, the tyrosine-phosphorylated receptors were immunoprecipitated by(More)
The effect of limited proteolysis of myosin subfragment I (S1) on conformational changes in F-actin during the formation of a rigor F-actin-S1 complex was studied, using polarized microfluorimetry. Upon the decoration of thin filaments made up of rhodaminyl-phalloin modified F-actin with subfragment I, the anisotropy of fluorescence increased. Limited(More)
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