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Ribonuclease |
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Ribonuclease A group of enzymes, widely distributed in nature, which catalyze hydrolysis of the internucleotide phosphodiester bonds in ribonucleic acid (RNA). The sites of hydrolysis may vary considerably, depending upon the specificity of the particular enzyme. Differences in specificity for the site of cleavage have led to the use of these various ribonucleases as tools in determining the structure and chemistry of RNA. See Enzyme, Nucleic acid Research on ribonuclease has played a prime role in advancing the understanding of protein structure and function; also, it was the first protein to be totally synthesized from its component amino acids. Since the elucidation of the amino acid sequence of ribonuclease, much information has been compiled with regard to the three-dimensional structure of the enzyme and to specific regions of the molecule which are catalytically important. See Protein How to thank TFD for its existence? Tell a friend about us, add a link to this page, add the site to iGoogle, or visit webmaster's page for free fun content. |
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| 5 [micro]g oligo(dT), 40 U recombinant ribonuclease inhibitor RNaseOUT (Invitrogen, Carlsbad, CA, USA), and variable amounts of cellular RNA and recRNA. To determine the exact phylogenetic relationship of the new isolate within the genus Bartonella, we analyzed an alignment that contained the sequences of 3 important phylogenetic markers, ribonuclease P RNA (RNase P RNA), 16S rDNA, and 23S rDNA, merged by catenation and organized by secondary structure elements, as described (5). When he and his colleagues compared the two ribonuclease genes, they found several differences that change the enzyme's amino acids. |
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