Title : [Studies on preferential binding to glucocorticoid of rat liver anionic glutathione S-transferase].

Pub. Date : 1985 Sep 20

PMID : 4085662






3 Functional Relationships(s)
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1 The dissociation constant of anionic GST-corticosterone complex was as low as 2.0 X 10(-8) M. Corticosterone inhibited the enzyme activity of anionic GST in a noncompetitive fashion with an apparent Ki value of 8.6 X 10(-5) M and 1.1 X 10(-6) M for 1-chloro-2.4-dinitrobenzene and GST respectively. Dinitrochlorobenzene hematopoietic prostaglandin D synthase Rattus norvegicus
2 The dissociation constant of anionic GST-corticosterone complex was as low as 2.0 X 10(-8) M. Corticosterone inhibited the enzyme activity of anionic GST in a noncompetitive fashion with an apparent Ki value of 8.6 X 10(-5) M and 1.1 X 10(-6) M for 1-chloro-2.4-dinitrobenzene and GST respectively. Dinitrochlorobenzene hematopoietic prostaglandin D synthase Rattus norvegicus
3 The dissociation constant of anionic GST-corticosterone complex was as low as 2.0 X 10(-8) M. Corticosterone inhibited the enzyme activity of anionic GST in a noncompetitive fashion with an apparent Ki value of 8.6 X 10(-5) M and 1.1 X 10(-6) M for 1-chloro-2.4-dinitrobenzene and GST respectively. Dinitrochlorobenzene hematopoietic prostaglandin D synthase Rattus norvegicus