Chemical characterization by protein sequence analysis of the bovine estrogen receptor.
Tryptic peptides generated from bovine estrogen receptor have been fractionated and purified using microbore column high performance liquid chromatography. Sequence analysis performed on six of these peptides, derived from diverse structural regions of the receptor protein, yielded 73 unique assignments corresponding to approximately 12% of the molecule. The amino acid sequences of these peptides displayed a high degree of similarity with corresponding sequences from estrogen receptors of mammalian origin, but were only moderately conserved in receptors from non-mammalian species. The sequenced residues of one tryptic peptide, positioned in the estrogen binding domain, were fully conserved in all estrogen receptors.
Ratajczak
T
T
Department of Obstetrics and Gynaecology, University of Western Australia, King Edward Memorial Hospital for Women, Subiaco.
Brockway
M J
MJ
Hähnel
R
R
Moritz
R L
RL
Simpson
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003600:Cytosol / Q000378:metabolism; D005260:Female; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011960:Receptors, Estrogen / Q000302:isolation & purification; D014357:Trypsin; D014599:Uterus / Q000378:metabolism
D010446:Peptide Fragments; D011960:Receptors, Estrogen; D014357:Trypsin