Title : Interaction of glucocorticoid receptor from rat liver with protamine and arginine.

Pub. Date : 1988 Jan

PMID : 3347046






7 Functional Relationships(s)
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1 The nontransformed glucocorticoid receptor (GR) from rat liver was found to bind to protamine-Sepharose and could be recovered by a salt gradient without a change in molecular configuration. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
2 The nontransformed glucocorticoid receptor (GR) from rat liver was found to bind to protamine-Sepharose and could be recovered by a salt gradient without a change in molecular configuration. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
3 The nontransformed GR also bound to arginine-Sepharose, but the transformed GR did not bind to either resin. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
4 The bindings of GR to protamine- and arginine-Sepharose were saturable. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
5 The apparent dissociation constants of GR on protamine-Sepharose varied from 0.34 nM (-molybdate) to 0.68 nM (+ 10 mM molybdate) and those on arginine-Sepharose were 1.99 nM (-molybdate) and 0.65 nM (+ 10mM molybdate), respectively. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
6 The apparent dissociation constants of GR on protamine-Sepharose varied from 0.34 nM (-molybdate) to 0.68 nM (+ 10 mM molybdate) and those on arginine-Sepharose were 1.99 nM (-molybdate) and 0.65 nM (+ 10mM molybdate), respectively. Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
7 Higher salt concentrations (0.5 M NaCl) were required to elute GR from protamine-Sepharose than from arginine-Sepharose (approx 0.03 M NaCl). Sepharose nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus