Structural studies of the estrogen receptor protein
MAb-Sepharose 6B only partially purified ER due to considerable nonspecific protein association. In some rat uterine preparations, both 65 and 50 kDa species were defined as ER proteins by Western Blot analysis using MAb-D547. A single ER species was also purified from MCF-7 human breast cancer cells grown in cell culture using these procedures. Diethylstilbestrol linked Sepharose 6B removed a 65 kDa ER and occasionally a 50 kDa protein. The 65 kDa preparation appeared homogeneous as ascertained by silver staining using either one or two dimensional gel electrophoresis. The 65 kDa ER from either type of affinity column using uterine preparations migrated as a single protein of identical isoelectric point and molecular weight. The 50 kDa ER which appeared in occasional preparations could not be induced by conditions that enhanced proteolysis indicating it may not be an artifact. A single 65 kDa species was identified on SDS-PAGE gels by autoradiography when either uterine tissue or MCF-7 cells were incubated with ({sup 32}P)orthophosphoric acid and isolated by affinity chromatography indicating phosphorylation of ER.
- Research Organization:
- Louisville Univ., KY (USA)
- OSTI ID:
- 5187892
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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ESTROGENS
RECEPTORS
PROTEIN STRUCTURE
CHROMATOGRAPHY
ELECTROPHORESIS
MOLECULAR WEIGHT
MONOCLONAL ANTIBODIES
PHOSPHORIC ACID
PHOSPHORUS 32
PHOSPHORYLATION
RATS
TRACER TECHNIQUES
TUMOR CELLS
UTERUS
ANIMAL CELLS
ANIMALS
ANTIBODIES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
FEMALE GENITALS
HORMONES
HYDROGEN COMPOUNDS
INORGANIC ACIDS
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAMMALS
MEMBRANE PROTEINS
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
PHOSPHORUS ISOTOPES
PROTEINS
RADIOISOTOPES
RODENTS
SEPARATION PROCESSES
STEROID HORMONES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques