COMPARATIVE-STUDIES ON RIBONUCLEASES BARNASE AND BINASE - HYBRID GENEAPPROACH

Authors
KURBANOV FT SHULGA AA RANJBAR B MAKAROV AA KIRPICHNIKOV MN
Citation
Ft. Kurbanov et al., COMPARATIVE-STUDIES ON RIBONUCLEASES BARNASE AND BINASE - HYBRID GENEAPPROACH, Molecular biology, 31(6), 1997, pp. 904-910
Citations number
22
Categorie Soggetti
Biology
Journal title
Molecular biology → ACNP
ISSN journal
00268933
Volume
31
Issue
6
Year of publication
1997
Pages
904 - 910
Database
ISI
SICI code
0026-8933(1997)31:6<904:CORBAB>2.0.ZU;2-M
Abstract
Hybrid RNases comprising segments of barnase (Ba) and binase (Bi): (1- 25)Ba/(26-110)Bi, (1-72)Ba/(73-110)Bi, (1-25)Ba/(26-72)Bi/(73-110)Ba, and (1-72)Bi/(73-110)Ba were compared in their catalytic properties wi th GpC, GpU, poly(A), and poly(I) as substrates. The nature of the C-p roximal part of the molecule (residues 73-110) was shown to determine not only the enzymic properties with low-molecular substrates but also the heat stability at acidic pH. On poly(I) the activity of the hybri ds was appreciably higher than that of binase, and was inversely corre lated with heat stability at near-neutral pH.