PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2785579-2 1989 Binding of 125I-labelled EGF to skin membrane particles was temperature- and time-dependent, with equilibrium being reached within 1 h at 23 degrees C. Analysis of skin biopsies collected from ten castrated Merino sheep demonstrated the presence of a single class of saturable, high-affinity binding sites with a dissociation constant of 64 +/- 4 (S.E.M.) Iodine-125 11-15 epidermal growth factor Mus musculus 25-28 2525915-2 1989 The binding of 125I-labelled EGF to hepatic membrane preparations of genetically diabetic mice was only 35% of that of non-diabetic mice. Iodine-125 15-19 epidermal growth factor Mus musculus 29-32 2789334-7 1989 Purified preparations of preproEGF (i) competed with 125I-labeled EGF for binding to the EGF receptor in intact fibroblast cells, (ii) activated the intrinsic tyrosine kinase activity of the EGF receptor in membrane preparations, and (iii) sustained the growth of a mouse keratinocyte cell line that is dependent on EGF for growth. Iodine-125 53-57 epidermal growth factor Mus musculus 31-34 2789334-7 1989 Purified preparations of preproEGF (i) competed with 125I-labeled EGF for binding to the EGF receptor in intact fibroblast cells, (ii) activated the intrinsic tyrosine kinase activity of the EGF receptor in membrane preparations, and (iii) sustained the growth of a mouse keratinocyte cell line that is dependent on EGF for growth. Iodine-125 53-57 epidermal growth factor Mus musculus 66-69 2785579-8 1989 Autoradiography of skin sections incubated with 125I-labelled EGF in vitro or of sections from skin which was perfused with 125I-labelled EGF in vivo demonstrated that EGF receptors were localized in undifferentiated cells of the epidermis and sebaceous glands, the inner and outer root sheath and bulb of wool follicles and in dermal arterioles. Iodine-125 48-52 epidermal growth factor Mus musculus 62-65 2785579-8 1989 Autoradiography of skin sections incubated with 125I-labelled EGF in vitro or of sections from skin which was perfused with 125I-labelled EGF in vivo demonstrated that EGF receptors were localized in undifferentiated cells of the epidermis and sebaceous glands, the inner and outer root sheath and bulb of wool follicles and in dermal arterioles. Iodine-125 124-128 epidermal growth factor Mus musculus 138-141 2785579-8 1989 Autoradiography of skin sections incubated with 125I-labelled EGF in vitro or of sections from skin which was perfused with 125I-labelled EGF in vivo demonstrated that EGF receptors were localized in undifferentiated cells of the epidermis and sebaceous glands, the inner and outer root sheath and bulb of wool follicles and in dermal arterioles. Iodine-125 124-128 epidermal growth factor Mus musculus 138-141 2785579-9 1989 Differences in receptor concentration were observed between follicles following in-vivo perfusion of 125I-labelled EGF but not when the in-vitro labelling technique was used. Iodine-125 101-105 epidermal growth factor Mus musculus 115-118 3493183-5 1987 We have now studied the quantity and pattern of EGF binding in teeth at various stages of development by incubating the dissected tooth germs with 125I-labeled EGF. Iodine-125 147-151 epidermal growth factor Mus musculus 48-51 3493183-5 1987 We have now studied the quantity and pattern of EGF binding in teeth at various stages of development by incubating the dissected tooth germs with 125I-labeled EGF. Iodine-125 147-151 epidermal growth factor Mus musculus 160-163 6323517-3 1984 All myometria (fundus) and leiomyomas and 3 of 4 endometria specifically bound 125I-labeled mouse EGF (myometria: mean, 1.1; range, 0.1-3.9 fmol/mg protein; leiomyomas: mean, 1.1; range, 0.2-2.6 fmol/mg protein; endometria: mean, 1.0; range, 0.0-3.1 fmol/mg protein). Iodine-125 79-83 epidermal growth factor Mus musculus 98-101 3157191-8 1985 The reduction of binding of 125I-labeled EGF by sn-1,2-dioctanoylglycerol was also time and dose dependent and appeared to result from a change in EGF affinity and not the number of receptor sites. Iodine-125 28-32 epidermal growth factor Mus musculus 41-44 3157191-8 1985 The reduction of binding of 125I-labeled EGF by sn-1,2-dioctanoylglycerol was also time and dose dependent and appeared to result from a change in EGF affinity and not the number of receptor sites. Iodine-125 28-32 epidermal growth factor Mus musculus 147-150 7438070-7 1980 The binding of 125I-labeled epidermal growth factor to the surface of mouse embryo fibroblasts, in contrast, was not affected. Iodine-125 15-19 epidermal growth factor Mus musculus 28-51 6287367-1 1982 Binding of 125I-labeled epidermal growth factor (EGF) to cells of cultured early postnatal mouse cerebellar cells was investigated by autoradiography in conjunction with cell type-specific immunolabeling of neurons, astrocytes and oligodendrocytes. Iodine-125 11-15 epidermal growth factor Mus musculus 24-47 6287367-1 1982 Binding of 125I-labeled epidermal growth factor (EGF) to cells of cultured early postnatal mouse cerebellar cells was investigated by autoradiography in conjunction with cell type-specific immunolabeling of neurons, astrocytes and oligodendrocytes. Iodine-125 11-15 epidermal growth factor Mus musculus 49-52 1055407-2 1975 It was assayed by its ability to compete with 125I-labeled mouse-derived epidermal growth factor in binding to human foreskin fibroblasts. Iodine-125 46-50 epidermal growth factor Mus musculus 73-96 6262576-3 1980 Furthermore, binding studies using 125I-labeled EGF have shown that the binding of EGF to the cell surface is reduced upon addition of succinylated concanavalin A. Iodine-125 35-39 epidermal growth factor Mus musculus 48-51 6262576-3 1980 Furthermore, binding studies using 125I-labeled EGF have shown that the binding of EGF to the cell surface is reduced upon addition of succinylated concanavalin A. Iodine-125 35-39 epidermal growth factor Mus musculus 83-86 7651906-1 1995 To test the stability of epidermal growth factor (EGF) in the gastrointestinal lumen 125I-labeled EGF was administered to the lumen of isolated stomach, duodenum, jejunum, midjejunum, and ileum of anesthetized mice (14-day-old neonatals and 8-week-old adults). Iodine-125 85-89 epidermal growth factor Mus musculus 98-101 1582020-0 1992 High-performance liquid chromatography of 125I-labeled mouse epidermal growth factor radioiodinated by six different methods. Iodine-125 42-46 epidermal growth factor Mus musculus 61-84 1576269-3 1992 Autoradiographic study demonstrated that the binding sites for 125I-labeled mouse EGF in the porcine ovary were present in the granulosa and luteal cells, but not in the thecal cells. Iodine-125 63-67 epidermal growth factor Mus musculus 82-85 1582020-1 1992 Six different procedures for radioiodination of mouse epidermal growth factor (EGF) all resulted in a heterogeneous 125I-labeled EGF preparation, as analyzed by reversed-phase HPLC. Iodine-125 116-120 epidermal growth factor Mus musculus 54-77 1582020-1 1992 Six different procedures for radioiodination of mouse epidermal growth factor (EGF) all resulted in a heterogeneous 125I-labeled EGF preparation, as analyzed by reversed-phase HPLC. Iodine-125 116-120 epidermal growth factor Mus musculus 79-82 1582020-1 1992 Six different procedures for radioiodination of mouse epidermal growth factor (EGF) all resulted in a heterogeneous 125I-labeled EGF preparation, as analyzed by reversed-phase HPLC. Iodine-125 116-120 epidermal growth factor Mus musculus 129-132 1582020-2 1992 EGF preparations that had been iodinated with Chloramine T, lodogen, or lodo-beads were found mainly to consist of oxidized 125I-labeled EGF moieties. Iodine-125 124-128 epidermal growth factor Mus musculus 0-3 1582020-2 1992 EGF preparations that had been iodinated with Chloramine T, lodogen, or lodo-beads were found mainly to consist of oxidized 125I-labeled EGF moieties. Iodine-125 124-128 epidermal growth factor Mus musculus 137-140 1582020-5 1992 This implies that HPLC purification of these 125I-labeled EGF preparations does not yield 125I-labeled EGF preparations with ligand equivalence. Iodine-125 45-49 epidermal growth factor Mus musculus 58-61 1582020-6 1992 However, all but one HPLC column fraction of Enzymobeads-125I-labeled EGF showed ligand equivalence. Iodine-125 57-61 epidermal growth factor Mus musculus 70-73 1582020-7 1992 Despite the small amount of the nonequivalent component in the Enzymobeads-labeled tracer, the nonchromatographed 125I-labeled EGF preparation showed ligand equivalence. Iodine-125 114-118 epidermal growth factor Mus musculus 127-130 1914179-4 1991 Scatchard analysis of competitive binding data (increasing concentrations of unlabeled EGF) obtained with commercially prepared 125I-labeled EGF (Chloramine T method), according to the specific radioactivity stated by the manufacturer, resulted in a substantial underestimation of the apparent number of receptors. Iodine-125 128-132 epidermal growth factor Mus musculus 87-90 1914179-4 1991 Scatchard analysis of competitive binding data (increasing concentrations of unlabeled EGF) obtained with commercially prepared 125I-labeled EGF (Chloramine T method), according to the specific radioactivity stated by the manufacturer, resulted in a substantial underestimation of the apparent number of receptors. Iodine-125 128-132 epidermal growth factor Mus musculus 141-144 1914179-7 1991 Scatchard plots of saturation and competitive binding data obtained with these 125I-labeled EGF preparations produced identical results for apparent receptor number and apparent dissociation constants. Iodine-125 79-83 epidermal growth factor Mus musculus 92-95 2015058-7 1991 The recombinant polypeptide was shown to compete with 125I-labelled mouse EGF for binding to cells and to stimulate DNA synthesis in quiescent monolayers of Swiss 3T3 cells. Iodine-125 54-58 epidermal growth factor Mus musculus 74-77 1832676-11 1991 In the presence of 1 microM bafilomycin A1, 125I-labeled epidermal growth factor (EGF) bound to the cell surface at 4 degrees C was internalized normally into the cells at 37 degrees C but was not degraded at all, in marked contrast to the rapid degradation of 125I-EGF in the control cells without the drug. Iodine-125 44-48 epidermal growth factor Mus musculus 57-80 1832676-11 1991 In the presence of 1 microM bafilomycin A1, 125I-labeled epidermal growth factor (EGF) bound to the cell surface at 4 degrees C was internalized normally into the cells at 37 degrees C but was not degraded at all, in marked contrast to the rapid degradation of 125I-EGF in the control cells without the drug. Iodine-125 44-48 epidermal growth factor Mus musculus 82-85 1832676-11 1991 In the presence of 1 microM bafilomycin A1, 125I-labeled epidermal growth factor (EGF) bound to the cell surface at 4 degrees C was internalized normally into the cells at 37 degrees C but was not degraded at all, in marked contrast to the rapid degradation of 125I-EGF in the control cells without the drug. Iodine-125 44-48 epidermal growth factor Mus musculus 266-269