TY - JOUR
T1 - A comparative study of electrophoretic mobilities of [3H]-estradiol and monohydroxytamoxifen binding components in the cytosols of human breast carcinomas and sera of healthy adult females
AU - Raam, Shanthi
AU - D'Agincourt, Paul G.
AU - Craig Jordan, V.
PY - 1983/10
Y1 - 1983/10
N2 - Cytosols from human breast carcinomas rich in estrogen receptors (ER) were examined for the presence of [3H]-estradiol (E2) and [3H]-monohydroxytamoxifen (OH-TX) binding components. Polyacrylamide gel electrophoresis was used to examine the comparative anodal mobilities of ER-[3H]-E2 and ER-[3H]-OH-TX complexes, and also to identify any cytosol or serum component that may exhibit preferential high affinity to OH-TX. We have demonstrated that [3H]-OH-TX binds ER with high affinity and the anodal mobility of ER-[3H]-OH-TX complexes is identical to that of ER-[3H]-E2 complexes. We were unable to identify an antiestrogen-specific component in ER-positive or ER-negative cytosols or in sera of healthy adult females. A serum component exhibiting a higher affinity to [3H]-OH-TX and [3H]-DES than to [3H]-E2 has been identified in all the female sera examined, but this binding is of high capacity and is unsaturable by a 1000-fold molar excess of unlabeled E2 or antiestrogens. The electrophoretic mobility of this component is comparable to that of serum albumin.
AB - Cytosols from human breast carcinomas rich in estrogen receptors (ER) were examined for the presence of [3H]-estradiol (E2) and [3H]-monohydroxytamoxifen (OH-TX) binding components. Polyacrylamide gel electrophoresis was used to examine the comparative anodal mobilities of ER-[3H]-E2 and ER-[3H]-OH-TX complexes, and also to identify any cytosol or serum component that may exhibit preferential high affinity to OH-TX. We have demonstrated that [3H]-OH-TX binds ER with high affinity and the anodal mobility of ER-[3H]-OH-TX complexes is identical to that of ER-[3H]-E2 complexes. We were unable to identify an antiestrogen-specific component in ER-positive or ER-negative cytosols or in sera of healthy adult females. A serum component exhibiting a higher affinity to [3H]-OH-TX and [3H]-DES than to [3H]-E2 has been identified in all the female sera examined, but this binding is of high capacity and is unsaturable by a 1000-fold molar excess of unlabeled E2 or antiestrogens. The electrophoretic mobility of this component is comparable to that of serum albumin.
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U2 - 10.1016/0277-5379(93)90016-X
DO - 10.1016/0277-5379(93)90016-X
M3 - Article
C2 - 6685632
AN - SCOPUS:0020561598
SN - 0277-5379
VL - 19
SP - 1457
EP - 1465
JO - European Journal of Cancer and Clinical Oncology
JF - European Journal of Cancer and Clinical Oncology
IS - 10
ER -