US EPA

1251636 

Journal Article 

Interaction of vanadyl ribonucleoside complex with the androgen receptor 

Ohara-Nemoto, Y; Yoshida, M; Ota, M 

1988 

Yes 

Biochemistry International
ISSN: 0158-5231 

17 

2 

197-202 

English 

3190719 

WOS:A1988P985600001 

The addition of vanadyl ribonucleoside complex (VRC), a potent inhibitor of RNase, to the transformed 4.5S androgen receptor from rat submandibular gland caused an increase in the sedimentation coefficient to 7.0S. Moreover, VRC decreased the DNA-cellulose binding of the transformed receptor; 50% inhibition of the DNA-cellulose binding was achieved at 1.8 mM VRC. On the other hand, agents related to VRC and oxoanions of transient metals, such as ribonucleoside, vanadate, molybdate, tungstate and arsenate, exerted no effect on the DNA-cellulose binding ability of the receptor. These findings suggest that VRC binds to the transformed androgen receptor at the DNA-binding site and that both oxovanadium ion and ribonucleoside are indispensable for the binding of VRC to the transformed androgen receptor.