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Non-Specific Depurination Activity of Saporin-S6, a Ribosome-Inactivating Protein, under Acidic Conditions
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S. Tang
Published/Copyright:
July 5, 2005
Abstract
Among five ribosome-inactivating proteins tested only saporin-S6 could efficiently release the adenine from adenosine 20 of the synthetic oligoribonucleotide (SRD RNA) mimic of the sarcin/ricin domain of rat 28S rRNA with a Km of 9μM and a kcat of approximately 0.4 min−1 at pH 7.6. The optimal pH for the depurination activity of saporin-S6 is 5.0. However, saporin-S6 lost its site-specificity of depurination on SRD RNA around the optimal pH. The non-specific depurination activity of saporin-S6 was dependent on the enzyme concentration and pH conditions. These results are valuable to understand the diversity and the depurination mechanism of ribosome-inactivating proteins.
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Published Online: 2005-07-05
Published in Print: 2000-08-06
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Highlight: Plant Biological Chemistry
- The Structural Properties of Plant Peroxisomes and Their Metabolic Significance
- Active Oxygen Species as Mediators of Plant Immunity: Three Case Studies
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- Topology Studies of the Chloroplast Protein Import Channel Toc75
- Plant Methionine Synthase: New Insights into Properties and Expression
- The Hepta-? -Glucoside Elicitor-Binding Proteins from Legumes Represent a Putative Receptor Family
- Octadecanoid and Jasmonate Signaling in Tomato (Lycopersicon esculentum Mill.) Leaves: Endogenous Jasmonates Do Not Induce Jasmonate Biosynthesis
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