The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates

Stable bovine RNase A aggregates larger than dimers (identified as trimers, tetramers, pentamers and hexamers) were obtained by lyophilization of RNase A from 40-50% acetic acid solutions. The RNase activity of these aggregates was compared with that of monomeric RNase A on single- and double-strand...

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Bibliographic Details
Published in:Biochemical journal 1996-08, Vol.318 ( Pt 1) (1), p.287-290
Main Authors: Libonati, M, Bertoldi, M, Sorrentino, S
Format: Article
Language:English
Subjects:
Animals
Biopolymers - metabolism
Cattle
Chromatography, Gel
Enzyme Stability
Nucleic Acid Conformation
Pancreas - enzymology
Poly A-U - metabolism
Poly U - metabolism
Protein Conformation
Ribonuclease, Pancreatic - chemistry
Ribonuclease, Pancreatic - metabolism
RNA, Double-Stranded - metabolism
Yeasts
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Summary:Stable bovine RNase A aggregates larger than dimers (identified as trimers, tetramers, pentamers and hexamers) were obtained by lyophilization of RNase A from 40-50% acetic acid solutions. The RNase activity of these aggregates was compared with that of monomeric RNase A on single- and double-stranded polyribonucleotides. Their activity toward poly(U) and yeast RNA slightly decreases as a function of the size of the aggregates. In contrast, their action on poly(A).poly(U) as substrate progressively increases from a relative activity of 1 for the RNase monomer to 10 for the hexamer. These results are discussed in the light of an already advanced hypothesis about a possible mechanism of RNase attack on double-stranded RNA.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3180287