Characterization of trypsin-treated forms of the estrogen receptor from rat and lamb uterus.
Characterization of trypsin-treated forms of the estrogen receptor from rat and lamb uterus.
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DOI:
10.1021/bi00638a025
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发表时间:
1977-09
期刊:
影响因子:
2.9
通讯作者:
K. Carlson;L. H. Sun;J. Katzenellenbogen
中科院分区:
文献类型:
--
作者:
K. Carlson;L. H. Sun;J. Katzenellenbogen
Kathryn E. Carlson, Lee-Hwei K. Sun, and John A. Katzenellenbogen* abstract: The molecular properties of uterine estrogen re-ceptors, following limited proteolysis, have been characterized. Mild trypsinization of cytoplasmic estrogen receptor prepa-rations from lamb and rat uterus causes a marked disaggre-gation of the receptor, giving lower molecular weight forms that retain unimpaired their ligand binding properties. These trypsinized receptorshave little tendency to reaggregate and thus are amenable to further purification and to detailed characterization. Sedimentation coefficients obtained by sucrose gradient centrifugation are 3.04±0.04 S for the lamb and 4.01±0.09 S for the rat trypsinized receptors; Stokes radii, determined bygel partition chromatography, are 2.76±0.23 nm for lamb and 2.94±0.25 nm for rat uterine re-ceptor. Discontinuous polyacrylamide gel electrophoresis in two systems (pH 7.8 and 10.2) shows the trypsinized lamb receptor as three distinct components (two major and one minor); the rat receptor is somewhat more disperse, but ap-