The antitumor action of seminal ribonuclease and its quaternary conformations

FEBS Letters

Bracale, Aurora¹  De Lorenzo, Claudia¹  Mastronicola, Maria Rosaria¹  Piccoli, Renata¹  D'Alessio, Giuseppe¹  Di Donato, Alberto¹  Cafaro, Valeria¹ 

[1] Dipartimento di Chimica Organica e Biologica, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy

关键词: Ribonuclease;    Antitumor;    Protein conformation;    Protein engineering;   

DOI  :  10.1016/0014-5793(94)01450-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has been previously shown that the antitumor action of bovine seminal ribonuclease (BS-RNase) is dependent on its dimeric structure. However, two distinct quaternary structures, each in equilibrium with the other, have been described for the enzyme: one in which the two subunits exchange their N-terminal ends, the other with no exchange. Antitumor activity assays, carried out on homogeneous quaternary forms of the enzyme, as well as on dimeric mutants of bovine pancreatic RNase A, reveal that another structural determinant of the antitumor activity of BS-RNase is the exchange of N-terminal ends between subunits.

【 授权许可】

Unknown