126. Physicochemical properties of native (N), trypsin treated (T) and calcium treated (Ca) calf uterus cytosol estrogen receptor at different steps of purification

Soulignac, O

doi:10.1016/0022-4731(74)90271-4

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“…Studies by Soulignac (1974 have indicated that trypsinization of the calf uterine estrogen receptor has little effect on its steroid binding properties. Although we have not done an exhaustive study, the steroid binding properties of the rat and lamb receptor also seem unaltered by trypsinization.…”

Section: Electrophoresis Of Androgen Receptors Has Been Performedmentioning

confidence: 99%

“…Although we have not done an exhaustive study, the steroid binding properties of the rat and lamb receptor also seem unaltered by trypsinization. However, after trypsinization, heat-activated receptor loses its ability to bind to nuclear constituents (Vallet-Strouve et al., 1974;Sala-Trepat and Vallet-Strouve, 1974); we have found this to be true for the lamb uterine receptor as well (K. E. Carlson, and J. A.…”

Section: Electrophoresis Of Androgen Receptors Has Been Performedmentioning

confidence: 99%

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Characterization of trypsin-treated forms of the estrogen receptor from rat and lamb uterus

Carlson¹,

Sun²,

Katzenellenbogen³

1977

Biochemistry

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Section: Electrophoresis Of Androgen Receptors Has Been Performedmentioning

confidence: 99%

Section: Electrophoresis Of Androgen Receptors Has Been Performedmentioning

confidence: 99%

Characterization of trypsin-treated forms of the estrogen receptor from rat and lamb uterus

Carlson¹,

Sun²,

Katzenellenbogen³

1977

Biochemistry

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Estrogen-Binding Sites of Chicken Liver. Preliminary Characterization of Nuclear Components

Gschwendt

Schneider

1978

Eur J Biochem

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1. Liver nuclei from estrogenized chickens contain high-affinity low-capacity estrogen-binding sites, which are in part salt-extractable (60 -70 %) and in part tightly sticking to the nuclear residue During the preparation of chromatin with low salt buffers part of the salt-extractable nuclearbinding sites remains together with the non-extractable sites on the chromatin. Extractable and non-extractable sites can be separated by agarose as well as hydroxyapatite chromatography.2. The estrogen-binding protein extracted from crude nuclei was characterized as follows : sedimentation coefficient of 3.9 S, Stokes' radius (a) of 3.3 nm, molecular weight ( M , ) of 56000 and frictional ratio (f/b) of 1.20. Trypsination results in a globular receptor fragment ( M , = 41 000), which has lost a small asymmetric portion of the receptor molecule but still binds estradiol.3. In contrast to the binding protein from crude nuclei the estrogen-binding protein extracted from purified nuclei at pH 7.4 is found mainly in an aggregated form. Dissociation of the aggregates is achieved in high saltlurea resulting in a receptor molecule with an apparent molecular weight of 130000. Aggregation of the binding sites can be prevented to some extent by raising the pH of the extraction medium. At pH 8.7 the non-aggregated part of the binding protein from pure nuclei could be characterized as follows: 4.4 S, a = 4.3 nm, M , = 80000 (apparent molecular weight of 4. Mixing experiments indicate that an extranuclear protease present in a crude nuclear preparation converts the large receptor (the binding protein from pure nuclei) to the smaller one (the binding protein from crude nuclei) by digesting off an asymmetric portion of the molecule. This portion seems to be responsible for the strong tendency of the binding protein from pure nuclei to associate with other nuclear components.(30-40%). 1500OO),fl'~ = 1.40.The chicken liver as site of the estrogen-induced egg yolk protein synthesis contains high-affinity lowcapacity estrogen-binding proteins in the cytosol [l] and in the nucleus [2-101. The number of nuclear binding sites is increased several-fold after estrogentreatment of the animals [2,6,8 -lo]. Most likely this is due to a translocation of the cytoplasmic estrogen-receptor complex to the nucleus [1,9]. These characteristics of the estrogen-binding in the chicken liver are in agreement with those of steroid hormonebinding in other target organs (for review see [ l l , 121). Part of the nuclear binding sites can be easily extracted from nuclei with salt-containing buffers [2 -4, 91, whereas part remains sticking to the chromatin Enzyme. Trypsin (EC 3.4.21.4).Triviaf Numes. Estradiol or estradiol-17a, 1,3,5(10)-estratriene-3,17b-diol; estradiol-I7a, 1,3,5(1O)-estratriene-3,17~-diol; estrone, 3-hydroxy-l,3,5(10)-estratriene-l7-one; diethylstilbestrol, 4,4-dihydroxy-trans-7,7'-diethylstilbene; testosterone, 17P-hydroxy-4-androsten-3-one; progesterone, 4-pregnene-3,20-dione; cortisol, 11b. 17a,21-trihydroxy-4-pregene-3,20-dione.

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126. Physicochemical properties of native (N), trypsin treated (T) and calcium treated (Ca) calf uterus cytosol estrogen receptor at different steps of purification

Cited by 2 publications

References 0 publications

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

Estrogen-Binding Sites of Chicken Liver. Preliminary Characterization of Nuclear Components

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