Characterization of Thermoactinomyces sacchari antigens
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چکیده
منابع مشابه
Isolation and characterization of host-selective toxin from Helminthosporium sacchari.
Helminthosporium sacchari infects certain clones of sugar cane and produces a toxin with the same plant selectivity as the fungus itself. The toxin was purified by use of activated charcoal plus thin layer, gel, and ion exchange chromatography. Gas chromatography (GC) of a trimethylsilyl derivative of toxin gave a single peak. Toxin was characterized by GC, mass spectroscopy (MS), and NMR spect...
متن کاملIsolation of bacteriophage from Thermoactinomyces.
Bacteriophages were isolated from strains of Thermoactinomyces vulgaris, T. candidus, and T. sacchari used to produce antigen for hypersensitivity pneumonitis screening at the Marshfield Medical Foundation. Whereas the one phage isolated from T. sacchari and two phages from T. vulgaris were species specific, three other phages isolated from T. vulgaris and the two phages isolated from T. candid...
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Thermoactinomyces vulgaris strain 5 produced two electrophoretically different alpha-amylases. Precipitation with ammonium sulfate and acetone did not alter the electrophoretic mobilities of either amylase isoenzyme. Patterns of the hydrolysis products of amylose by the two amylase isoenzymes were essentially identical.
متن کاملThermoactinomyces Tsiklinsky, a genus of thermophilic actinomycetes.
There has been considerable confusion concerning the nature and classification of thermophilic actinomycetes. Beginning with the early studies of Kedzoir (1896), Berestnev (1897), Tsiklinsky (1899), Gilbert (1904), and Miehe (1907), it was recognized that the actinomycetes capable of growing at higher temperatures (50 to 65 C) represent two distinct groups or types: (1) One group produces a tru...
متن کاملPurification, characterization, and subsite affinities of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylases.
A maltooligosaccharide-metabolizing enzyme from Thermoactinomyces vulgaris R-47 (TGA) homologous to glucoamylases does not degrade starch efficiently unlike most glucoamylases such as fungal glucoamylases (Uotsu-Tomita et al., Appl. Microbiol. Biotechnol., 56, 465-473 (2001)). In this study, we purified and characterized TGA, and determined the subsite affinities of the enzyme. The optimal pH a...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1978
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.20.2.519-525.1978