FULL ANTITUMOR ACTION OF RECOMBINANT SEMINAL RIBONUCLEASE DEPENDS ON THE REMOVAL OF ITS N-TERMINAL METHIONINE

Citation
Bs. Adinolfi et al., FULL ANTITUMOR ACTION OF RECOMBINANT SEMINAL RIBONUCLEASE DEPENDS ON THE REMOVAL OF ITS N-TERMINAL METHIONINE, Biochemical and biophysical research communications, 213(2), 1995, pp. 525-532
Citations number
23
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006-291X
Volume
213
Issue
2
Year of publication
1995
Pages
525 - 532
Database
ISI
SICI code
0006-291X(1995)213:2<525:FAAORS>2.0.ZU;2-V
Abstract
Bovine seminal RNase (BS-RNase) is a dimeric member of the pancreatic- like ribonuclease superfamily, with antitumor activity. We report here that recombinant Met(-1) BS-RNase is a less potent cytotoxic factor, while structurally and catalytically indistinguishable from BS-RNase i solated from natural sources. Mature recombinant BS-RNase instead disp lays full antitumor action. This suggests that the conformation of the N-terminal region of BS-RNase is among the structural determinants of its antitumor action, in addition to its catalytic activity and its q uaternary structure. (C) 1995 Academic Press, Inc.