The Experts below are selected from a list of 96 Experts worldwide ranked by ideXlab platform
M. Catherine Aime - One of the best experts on this subject based on the ideXlab platform.
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A new lineage in Pucciniomycotina: class Tritirachiomycetes, order Tritirachiales, family Tritirachiaceae
Mycologia, 2011Co-Authors: Wiley A. Schell, Arthur G. Lee, M. Catherine AimeAbstract:Based on multiple gene analyses (nuclear large subunit, nuclear small subunit, internal transcribed spacer region including the 5.8 s subunit rDNA, and translation elongation factor 1α) and septal pore ultrastructure we describe a new lineage of Pucciniomycotina consisting of a new class, Tritirachiomycetes, new order, Tritirachiales, and new family, Tritirachiaceae. Tritirachium dependens, T. oryzae, T. roseum (reintroduced), T. cinnamomeum and two unidentified species are recognized. Phylogenetic analyses do not support existing morphological circumscription of some species, and the available evidence suggests that morphological evaluation alone is not adequate for species identification.
Wiley A. Schell - One of the best experts on this subject based on the ideXlab platform.
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A new lineage in Pucciniomycotina: class Tritirachiomycetes, order Tritirachiales, family Tritirachiaceae
Mycologia, 2011Co-Authors: Wiley A. Schell, Arthur G. Lee, M. Catherine AimeAbstract:Based on multiple gene analyses (nuclear large subunit, nuclear small subunit, internal transcribed spacer region including the 5.8 s subunit rDNA, and translation elongation factor 1α) and septal pore ultrastructure we describe a new lineage of Pucciniomycotina consisting of a new class, Tritirachiomycetes, new order, Tritirachiales, and new family, Tritirachiaceae. Tritirachium dependens, T. oryzae, T. roseum (reintroduced), T. cinnamomeum and two unidentified species are recognized. Phylogenetic analyses do not support existing morphological circumscription of some species, and the available evidence suggests that morphological evaluation alone is not adequate for species identification.
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Short title: Tritirachiomycetes: a new lineage A new lineage in Pucciniomycotina: class Tritirachiomycetes, order Tritirachiales, family Tritirachiaceae
2011Co-Authors: Wiley A. Schell, Arthur G. Lee, M. CatherineAbstract:Based on multiple gene analyses (nuclear large subunit, nuclear small subunit, internal transcribed spacer region including the 5.8s subunit rDNA, and translational elongation factor 1α) and septal pore ultrastructure we describe a new lineage of Pucciniomycotina consisting of a new class, Tritirachiomycetes, new order, Tritirachiales, and new family, Tritirachiaceae. Tritirachium dependens, T. oryzae, T. roseum (reintroduced), T. cinnamomeum and two unidentified species are recognized. Phylogenetic analyses do not support existing morphological circumscription of some species, and the available evidence suggests that morphological evaluation alone is not adequate for species identification.
Arthur G. Lee - One of the best experts on this subject based on the ideXlab platform.
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A new lineage in Pucciniomycotina: class Tritirachiomycetes, order Tritirachiales, family Tritirachiaceae
Mycologia, 2011Co-Authors: Wiley A. Schell, Arthur G. Lee, M. Catherine AimeAbstract:Based on multiple gene analyses (nuclear large subunit, nuclear small subunit, internal transcribed spacer region including the 5.8 s subunit rDNA, and translation elongation factor 1α) and septal pore ultrastructure we describe a new lineage of Pucciniomycotina consisting of a new class, Tritirachiomycetes, new order, Tritirachiales, and new family, Tritirachiaceae. Tritirachium dependens, T. oryzae, T. roseum (reintroduced), T. cinnamomeum and two unidentified species are recognized. Phylogenetic analyses do not support existing morphological circumscription of some species, and the available evidence suggests that morphological evaluation alone is not adequate for species identification.
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Short title: Tritirachiomycetes: a new lineage A new lineage in Pucciniomycotina: class Tritirachiomycetes, order Tritirachiales, family Tritirachiaceae
2011Co-Authors: Wiley A. Schell, Arthur G. Lee, M. CatherineAbstract:Based on multiple gene analyses (nuclear large subunit, nuclear small subunit, internal transcribed spacer region including the 5.8s subunit rDNA, and translational elongation factor 1α) and septal pore ultrastructure we describe a new lineage of Pucciniomycotina consisting of a new class, Tritirachiomycetes, new order, Tritirachiales, and new family, Tritirachiaceae. Tritirachium dependens, T. oryzae, T. roseum (reintroduced), T. cinnamomeum and two unidentified species are recognized. Phylogenetic analyses do not support existing morphological circumscription of some species, and the available evidence suggests that morphological evaluation alone is not adequate for species identification.
Babru B Samal - One of the best experts on this subject based on the ideXlab platform.
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cloning and expression of the gene encoding a novel proteinase from Tritirachium album limber
Advances in Experimental Medicine and Biology, 1996Co-Authors: Babru B Samal, T Boone, B Karan, K Chen, R Sachdev, T ArakawaAbstract:We have isolated the cDNA and the genomic clones encoding a novel serine proteinase, named proteinase T, from the fungus Tritirachium album Limber. The coding region of the gene is interrupted by two introns. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K. Four cysteines are present in the mature proteinase, probably in the form of disulfide bonds. We have also purified the native proteinase from Tritirachium album Limber grown in the presence of 2% skim milk. Proteinase T is extremely stable at 50 degrees C. The thermal stability is not affected in the presence of 1% SDS either at pH 8.0 or 10.0. We have expressed the cDNA of proteinase T in Escherichia coli. The authenticity of the proteinase has been characterized by Western blotting and amino terminal analysis of the recombinant product. High level expression of proteinase T in E. coli as well as the refolding process to generate active proteinase will be discussed in detail.
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isolation and thermal stability studies of two novel serine proteinases from the fungus Tritirachium album limber
Enzyme and Microbial Technology, 1991Co-Authors: Babru B Samal, B Karan, Carol Parker, Yitzhak StabinskyAbstract:A number of serine proteinases are secreted into the culture medium when Tritirachium album Limber is supplied with protein as the only nitrogen source. From this population of proteinases, we have isolated two novel proteolytic enzymes, designated as proteinase R and T. We have compared the thermal stability of these two proteinases with that of subtilisin BPN' and proteinase K. Both of these proteinases were thermally stable in the absence of detergents in buffers of low (4.0) and high (10.0) pH. The thermal stability of proteinase T was not affected by the presence of 1.0% SDS either at pH 8.0 or 10.0 in contrast to proteinase R which became heat labile. At low pH, the presence of SDS was detrimental to the stability of all the proteinases.
Yitzhak Stabinsky - One of the best experts on this subject based on the ideXlab platform.
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isolation and thermal stability studies of two novel serine proteinases from the fungus Tritirachium album limber
Enzyme and Microbial Technology, 1991Co-Authors: Babru B Samal, B Karan, Carol Parker, Yitzhak StabinskyAbstract:A number of serine proteinases are secreted into the culture medium when Tritirachium album Limber is supplied with protein as the only nitrogen source. From this population of proteinases, we have isolated two novel proteolytic enzymes, designated as proteinase R and T. We have compared the thermal stability of these two proteinases with that of subtilisin BPN' and proteinase K. Both of these proteinases were thermally stable in the absence of detergents in buffers of low (4.0) and high (10.0) pH. The thermal stability of proteinase T was not affected by the presence of 1.0% SDS either at pH 8.0 or 10.0 in contrast to proteinase R which became heat labile. At low pH, the presence of SDS was detrimental to the stability of all the proteinases.
