Sequence analysis of the nonsteroid binding component of the calf uterine estrogen receptor.
Microbore reversed-phase high performance liquid chromatography has been utilized to fractionate and purify a number of tryptic peptides generated from the 90K nonsteroid binding component of the calf uterine estrogen receptor. Sequence analysis was performed on six peptides yielding 78 unique amino acid assignments, this corresponds to approximately 10% of the molecule. These peptides share sequence similarities with three heat shock proteins, Drosophila hsp 83 (83% homologous), yeast hsp 90 (55%) and chicken hsp 108 (32%). The amino acid composition of the protein indicates a prevalence of charged amino acid residues.
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; D001665:Binding Sites; D002417:Cattle; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D004330:Drosophila; D005260:Female; D006360:Heat-Shock Proteins / Q000032:analysis; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011960:Receptors, Estrogen / Q000032:analysis*; D011980:Receptors, Progesterone / Q000032:analysis; D014357:Trypsin / Q000378:metabolism; D014599:Uterus / Q000032:analysis*
D006360:Heat-Shock Proteins; D011960:Receptors, Estrogen; D011980:Receptors, Progesterone; D014357:Trypsin