A physical map of the sulfur-dependent archaebacterium Sulfolobus acidocaldarius 7 chromosome
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منابع مشابه
Circular chromosomal DNA in the sulfur-dependent archaebacterium Sulfolobus acidocaldarius.
The shape of the chromosomal DNA of the sulfur-dependent archaebacterium Sulfolobus acidocaldarius was analyzed by the pulsed-field gel electrophoresis(PFGE). S.acidocaldarius DNA digested with Notl showed two DNA bands at around 1.0 Mbp and 2.1 Mbp. Notl-linking clones were isolated from the library of S.acidocaldarius chromosomal DNA. It contained two Notl sites. Both 1.0 and 2.1 Mbp DNA band...
متن کاملHigh Efficiency of Plating of the Thermophilic Sulfur-Dependent Archaebacterium Sulfolobus acidocaldarius.
A procedure for plating Sulfolobus acidocaldarius using Gelrite as the gelling agent is presented. The technique uses a supporting gel of 0.8% (wt/vol) Gelrite and an overlay soft gel of 0.4% (wt/vol) Gelrite, in which the colonies are grown. The plating efficiency was essentially 100%.
متن کاملDNA-dependent RNA polymerase from the archaebacterium Sulfolobus acidocaldarius.
Purified DNA-dependent RNA polymerase from Sulfolobus acidocaldarius is composed of 10 different subunits, one of which is present as four copies. Their molecular weights are 122 000, 101 000, 44 000, 32 000, 24 000, 17 500, 13 800, 11 800 (four copies), 11 200, 10 800, summing up to a total Mr of 423 500. The sedimentation velocity is 13.5 S, indicating that at 0.5 M NH4Cl the enzyme exists in...
متن کاملGlycogen-bound polyphosphate kinase from the archaebacterium Sulfolobus acidocaldarius.
Glycogen-bound polyphosphate kinase has been isolated from a crude extract of Sulfolobus acidocaldarius by isopycnic centrifugation in CsCl. Divalent cations (Mn2+ greater than Mg2+) stimulated the reaction. The enzyme does not require the presence of histones for its activity; it is inhibited strongly by phosphate and slightly by fluoride. The protein from the glycogen complex migrated in a so...
متن کاملPurification and characterization of a heat-stable esterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.
A heat-stable esterase has been purified 1080-fold to electrophoretic homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium; 20% of the starting activity is recovered. The purified enzyme shows a specific activity of 158 units/mg, based on the hydrolysis of p-nitrophenyl acetate. The esterase hydrolyses short-chain p-nitrophenyl esters, aliphatic esters and triacylglyc...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1993
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.175.5.1532-1536.1993