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Title: Physicochemical properties and amino acid composition of highly purified preparation of distinctive estrogen-binding protein from rat liver

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5726913

The structure and properties of a distinctive estrogen-binding protein (DEBP) from the livers of male rats, purified with the aid of an affinity sorbent, was investigated. A high degree of purification of the DEBP obtained (> 99%), associated with the pronounced microheterogeneity, was found. Apparently, this microheterogeneity is the result of partial proteolysis of the protein from the N-end during isolation. Purified DEBP molecules have the following parameters: molecular weight 31,000 (according to the data of electrophoresis in polyacrylamide gel in the presence of SDS), sedimentation coefficient 3.765, Stokes' radius 25.6 A, frictional ratio 1.11. Absorption maximum of the protein in the ultraviolet region 276 nm; extinction coefficient 26; content of ..cap alpha..-helical segments 25-30%. The equilibrium constant of the association with estradiol is 5 x 10/sup 7/ M/sup -1/. Estriol (> 100%) and, to a lesser degree, estrone and testosterone (approx. 10%) compete for the protein-binding sites on (/sup 3/H) estradiol, whereas androsterone has practically no competitive effect. A study of the amino acid composition of the DEBP showed that the protein contains a large number of residues with hydrophobic side groups (34.4%), it has more acidic than basic amino acids, and possesses a low content of cysteine, threonine, and histidine.

Research Organization:
Lomonosov Moscow State Univ., Moscow (Russian Federation)
OSTI ID:
5726913
Journal Information:
Biochemistry (Engl. Transl.); (United States), Vol. 51:6; Other Information: Translated from Biokhimiya; 51: 6, 958-966(Jun 1986)
Country of Publication:
United States
Language:
English

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