Interaction of bovine estrogen receptor with immobilized zinc

Journal Article · Sat Sep 01 04:00:00 EDT 1990 · Steroids; (USA)

DOI:https://doi.org/10.1016/0039-128X(90)90099-W· OSTI ID:5889515

Atkinson, H C; Ratajczak, T; Haehnel, R ^[1]

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1. Univ. of Western Australia, Subiaco (Australia)

The metal-binding properties of partially purified untransformed or salt-dissociated bovine estrogen receptors were studied using zinc-chelated iminodiacetic acid gels. Only the salt-dissociated 5S receptor is retained by the metal-chelated resin, and this interaction is dependent on the presence of dithiothreitol. The untransformed 9S receptor is not retained, indicating that the zinc-interacting amino acid residues may be masked by receptor-associated proteins such as 90K heat-shock protein or because of an unfavorable receptor conformation.

• OSTI ID: 5889515
• Journal Information: Steroids; (USA), Journal Name: Steroids; (USA) Vol. 55:9; ISSN 0039-128X; ISSN STEDA
• Country of Publication: United States
• Language: English

Related Subjects

560300* -- Chemicals Metabolism & Toxicology
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
AMINO ACIDS
ANIMALS
BIOCHEMICAL REACTION KINETICS
CARBOXYLIC ACIDS
CATTLE
CENTRIFUGATION
CHELATING AGENTS
CHEMICAL PROPERTIES
DOMESTIC ANIMALS
ELEMENTS
ESTROGENS
HORMONES
KINETICS
MAMMALS
MEMBRANE PROTEINS
METABOLISM
METALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
REACTION KINETICS
RECEPTORS
RUMINANTS
SEPARATION PROCESSES
STEROID HORMONES
ULTRACENTRIFUGATION
VERTEBRATES
ZINC