Steroid binding domain of porcine estrogen receptor

Journal Article · Tue May 05 04:00:00 EDT 1987 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00383a023· OSTI ID:5850956

Koike, S; Nii, A; Sakai, M; Muramatsu, M

For the purpose of characterizing the estrogen binding domain of porcine estrogen receptor (ER), the authors have made use of affinity labeling of partially purified ER with (/sup 3/H)tamoxifen aziridine. The labeling is very efficient and selective particularly after partial purification of ER. A 65,000-dalton (65-kDa) band was detected on the fluorogram of a sodium dodecyl sulfate-polyacrylamide gel, together with a 50-kDa band and a few more smaller bands. The 50-kDa protein appears to be a degradation product of the 65-kDa protein in view of the similar peptide map. ER was affinity labeled before or after controlled limited proteolysis with either trypsin, papain, or ..cap alpha..-chymotrypsin. The labeling patterns of limited digests indicate that a fragment of about 30 kDa is relatively resistant to proteases and has a full and specific binding activity to estrogen, whereas smaller fragments have lost much of the binding activity. This fragment is very hydrophobic and probably corresponds to the carboxy half of ER.

• Research Organization: Univ. of Tokyo, Japan
• OSTI ID: 5850956
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:9; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ANIMALS
BODY
CHEMICAL REACTIONS
CONFIGURATION INTERACTION
DECOMPOSITION
DOMESTIC ANIMALS
ELECTROPHORESIS
ENZYMATIC HYDROLYSIS
ESTRADIOL
ESTRANES
ESTROGENS
FEMALE GENITALS
HORMONES
HYDROLYSIS
HYDROXY COMPOUNDS
LABELLED COMPOUNDS
LYSIS
MAMMALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RECEPTORS
SOLVOLYSIS
STEROID HORMONES
STEROIDS
SWINE
TRITIUM COMPOUNDS
UTERUS
VERTEBRATES