Zobrazeno 1 - 10
of 47
pro vyhledávání: '"S. I. Bezborodova"'
Autor:
S I, Bezborodova
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 27(3)
The recent discovery of unexpected functional diversity of different RNA molecules and some products of their degradation renewed the interest in ribonucleases. This review mainly presents recent systematized data on animal ribonucleases, including p
Publikováno v:
Collection of Czechoslovak Chemical Communications. 39:993-1004
Autor:
Antonín Holý, N. M. Abrosimova-Amelyanchik, S. I. Bezborodova, R. I. Tatarskaya, G. S. Ivanova, E. Zelinková
Publikováno v:
Collection of Czechoslovak Chemical Communications. 39:2986-2997
Publikováno v:
Mikrobiologiia. 45(2)
Autor:
V I, Krupianko, S I, Bezborodova
Publikováno v:
Biokhimiia (Moscow, Russia). 41(8)
In studies of splitting of transferase substrates cytidylyl-(3' leeds to 5')-adenosine and adenylyl-(3'leds to to 5')-cytidine by Penicillium brevicompactum RNAase the pH-optimum activity of enzyme has been found to fall within the range of 4.7 +/- 0
Autor:
N Iu, Markelova, S I, Bezborodova
Publikováno v:
Nauchnye doklady vysshei shkoly. Biologicheskie nauki. (5)
Publikováno v:
Bioorganicheskaia khimiia. 14(7)
Extracellular RNase Fl1 has been purified from the culture filtrate of Fusarium lateritium. The enzyme has been obtained in the electrophoretically homogeneous state with the yield about 90% and 300 fdd degree of purification. RNase Fl1 is a guanyl s
Publikováno v:
Bioorganicheskaia khimiia. 14(5)
The complete amino acid sequence of an extracellular guanyl-specific RNase from Aspergillus pallidus fungi has been established. The RNase contains 104 amino acid residues (Mr 11,029). Its primary structure was analyzed basing on the automated Edman
Publikováno v:
Biokhimiia (Moscow, Russia). 53(6)
Extracellular guanyl-specific RNAase of the fungus Aspergillus pallidus (RNAase ApI) was isolated in preparative amounts with a 40% yield and purified to homogeneity (938-fold). The complete amino acid sequence of the protein (104 amino acid residues
Publikováno v:
Biokhimiia (Moscow, Russia). 42(9)
The purification of RNase C2 from 76.5 1 of Asp. clavatus cultural fluid and RNase Pch1 from 160 1 of Pen. chrysogenum 152 A cultural fluid was described. 1150-fold purification of RNase C2 was attained by precipitation with ammonium sulfate, ion-exc