Kinetics of in vitro binding of oestradiol in subcellular fractions of testicular and uterine tissue: Characterization of oestradiol binding in testicular nuclei

1977 ◽  
Vol 8 (8) ◽  
pp. 859-865 ◽  
Author(s):  
Willem De Boer ◽  
Joan De Vries ◽  
Eppo Mulder ◽  
Henk J. Van Der Molen
Keyword(s):  
Tissue Characterization ◽  
Subcellular Fractions ◽  
Uterine Tissue ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Kinetics Of

Characterization of the in vitro Binding of [3H] DP-5,6-ADTN to Rat Striatal Membranes

1986 ◽  
pp. 405-406
Author(s):  
T. B. A. Mulder ◽  
C. J. Grol ◽  
D. Dijkstra ◽  
A. S. Horn
Keyword(s):  
In Vitro Binding ◽  
Vitro Binding

scholarly journals PEROXIDASE-ASSOCIATED BINDING OF ESTRADIOL BY THE RAT UTERUS

1969 ◽  
Vol 17 (6) ◽  
pp. 394-407 ◽  
Author(s):  
JOST BRÖKELMANN
Keyword(s):  
Hydrogen Peroxide ◽  
Incubation Medium ◽  
Degradation Products ◽  
Uterine Tissue ◽  
Electron Microscopic ◽  
Rat Uterus ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Specific Granules

It has been shown that the addition of hydrogen peroxide to the incubation medium greatly increases the in vitro binding of tritiated estradiol or its degradation products to uterine tissue. The binding probably is covalent. It involves a hemoprotein which can be demonstrated histochemically by a peroxidase reaction. In light and electron microscopic radioautographs, the sites of radioactivity in uterine tissues after incubation with tritiated estradiol are mainly the specific granules of eosinophils and the cytoplasm of epithelial cells. The possible significance of an interaction between estradiol and a peroxidative hemoprotein is discussed.

Characterization of anti oLHβ-antibodies acting as contraceptives in rhesus monkeys. I. In vitro binding properties

1982 ◽  
Vol 4 (5) ◽  
pp. 295-311 ◽  
Author(s):  
Yukio Yamamoto ◽  
Glen L. Gunsalus ◽  
Kalyan Sundaram ◽  
Rosemarie B. Thau
Keyword(s):  
Rhesus Monkeys ◽  
Binding Properties ◽  
In Vitro Binding ◽  
Vitro Binding

scholarly journals Characterization of Influenza Virus PB1 Protein Binding to Viral RNA: Two Separate Regions of the Protein Contribute to the Interaction Domain

1999 ◽  
Vol 73 (1) ◽  
pp. 631-637 ◽  
Author(s):  
Susana González ◽  
Juan Ortín
Keyword(s):  
Influenza Virus ◽  
Experimental Approach ◽  
Viral Rna ◽  
Deletion Mutants ◽  
Interaction Domain ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
In Vitro Interaction

ABSTRACT The interaction of the PB1 subunit of the influenza virus polymerase with the viral RNA (vRNA) template has been studied in vitro. The experimental approach included the in vitro binding of labeled model vRNA to PB1 protein immobilized as an immunoprecipitate, as well as Northwestern analyses. The binding to model vRNA was specific, and an apparent Kd of about 2 × 10−8 M was determined. Although interaction with the isolated 3′ arm of the panhandle was detectable, interaction with the 5′ arm was prominent and the binding was optimal with a panhandle analog structure (5′+3′ probe). When presented with a panhandle analog mixed probe, PB1 was able to retain the 3′ arm as efficiently as the 5′ arm. The sequences of the PB1 protein involved in vRNA binding were identified by in vitro interaction tests with PB1 deletion mutants. Two separate regions of the PB1 protein sequence proved positive for binding: the N-terminal 83 amino acids and the C-proximal sequences located downstream of position 493. All mutants able to interact with model vRNA were capable of binding the 5′ arm more efficiently than the 3′ arm of the panhandle. Taken together, these results suggest that two separate regions of the PB1 protein constitute a vRNA binding site that interacts preferentially with the 5′ arm of the panhandle structure.

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