Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The major birch (Betula alba L.) pollen allergen, Bet v 1, has been shown to be homologous to pathogenesis-related proteins in a number of plants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley and to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was separated in an RNase activity gel. Four major RNase bands were excised from the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by Western blotting with a specific Bet v 1 monoclonal antibody and patient's serum. Thus the monomer and the dimer of Bet v 1 showed RNase activity. Purified recombinant Bet v 1 was shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units.mg-1.
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PMID:The major birch pollen allergen, Bet v 1, shows ribonuclease activity. 877 1

Maximum accumulation of Pin m III protein in western white pine (Pinus monticola Dougl. ex D. Don) needles occurred during the winter months. To characterize Pin m III, an expression cDNA library from poly(A)+ mRNA of needles was immunoscreened and the full length cDNA was cloned. An open reading frame of 486 bases encodes a protein of 161 amino acid residues with a molecular mass of 18 kD and a predicted isoelectric point of 5.5. The deduced amino acid sequence had some similarities (37%) with an intracellular pathogenesis-related (PR) protein from garden asparagus (Asparagus officinalis L.) and the major pollen allergen from white birch (Betula verrucosa J. F. Ehrh.), which are members of the ribonuclease-like PR-10 family. Phylogenetic analysis provided circumstantial evidence that Pin m III may be grouped with intracellular PRs from asparagus and potato (Solanum tuberosum L.), while the allergens formed another subgroup. Northern analysis showed that the Pin m III gene was preferentially expressed during cold acclimation with the highest expression in the fall and winter months, preceding the peak of Pin m III protein accumulation. Tissue specificity expression analysis indicated that the gene was strongly expressed in roots and twigs. Higher amounts of the homologous protein (Pin l I) and its transcript accumulated in sugar pine (Pinus lambertiana Dougl.) needles infected with blister rust compared with healthy needles.
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PMID:Characterization of Pin m III cDNA in western white pine. 1265 16