Results 271 to 280 of about 315,883 (294)

Processing yeast to reduce its nucleic acid content. Induction of intracellular RNase action by a simple heat‐shock procedure, and an efficient chemical method based on extraction of RNA by salt solutions at low pH

Journal of the Science of Food and Agriculture, 1978
AbstractAutolytic breakdown of the RNA of Saccharomyces cerevisiae can be induced by subjecting a suspension of yeast in NaCl solution at pH 6 to heat shock, produced by bringing the suspension to 50°C and then adding enough water at 100°C to increase the temperature momentarily to 68°C, followed after 1 min by the addition of cold water to reduce it ...
William E. Trevelyan
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Cleavage Site Selection by M1 RNA, the Catalytic Subunit of Escherichia coli RNase P, is influenced by pH

Journal of Molecular Biology, 1994
We have studied cleavage site selection by M1 RNA, the catalytic subunit of Escherichia coli RNase P, under various reaction conditions using tRNA precursors which are cleaved at two positions. Our results showed that the preference of cleavage site changed with variations in pH or Mg2+ concentration.
Joanna Kufel, Leif A. Kirsebom
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[68] Preparation of bacterial DNA by the phenol-pH 9-RNases method

, 1967
Publisher Summary This chapter describes the method for the extraction of DNA from bacterial cells using phenol. Phenol treatment is considered one of the most effective methods for deproteinization. Whereas a neutral or acidic buffer (pH 5-7) extracts RNA into aqueous phase, rather than DNA from bacterial cells, in phenol treatment slightly alkaline
Kin‐ichiro Miura
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The pH-dependence of the Escherichia coli RNase HII-catalysed Reaction Suggests that an Active Site Carboxylate Group Participates Directly in Catalysis

Journal of Molecular Biology, 2007
RNase HII specifically catalyses the hydrolysis of phosphate diester linkages contained within the RNA portion of DNA/RNA hybrids. The catalytic parameters of the enzyme derived from Escherichia coli BL21 have been measured using 5'-fluorescent oligodeoxynucleotide substrates containing embedded ribonucleotides.
James A. Bastock, Michelle Webb, Jane A. Grasby   +2 more
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pH Dependence of the RNase T1 Action on Nucleoside 2′ 3′-Cyclic Phosphates

The Journal of Biochemistry, 1970
Shinkichi Irie, Tokuo Itoh, Tohru Ueda, Fujio Egami   +3 more
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Extracellular Saline, RNase-Free (1×, pH 7.3)

Cold Spring Harbor Protocols, 2014

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Simulation Analysis of the Binding Interactions in the RNase A/3'-UMP Enzyme-Product Complex as a Function of pH

Journal of the American Chemical Society, 1994
John E. Straub, Carmay Lim, Martin Karplus   +2 more
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RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3′ end of RNA

Biochimie, 1990
Escherichia coli RNase PH is a phosphate-dependent exoribonuclease that has been implicated in the 3' processing of tRNA precursors. It degrades RNA chains in a phosphorolytic manner releasing nucleoside diphosphates as products. Here we show that RNase PH also catalyzes a synthetic reaction, the addition of nucleotides to the 3' termini of RNA ...
K A, Ost, M P, Deutscher
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The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

Cancer Letters, 2007
TCL1 is an AKT kinase coactivator that, when dysregulated, initiates mature lymphocyte malignancies in humans and transgenic mice. While TCL1 augments AKT pathway signaling, additional TCL1 interacting proteins that may contribute to cellular homeostasis or transformation are lacking.
Samuel W, French, David W, Dawson, Hsiao-Wen, Chen, Robert N, Rainey, Stuart A, Sievers, Cynthia E, Balatoni, Larry, Wong, Joshua J, Troke, Mai T N, Nguyen, Carla M, Koehler, Michael A, Teitell   +10 more
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Atomic resolution structures of rnase A at six ph values

2002
The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-
SICA, FILOMENA, MAZZARELLA, LELIO, ZAGARI, ADRIANA, LAMZIN V. S., WILSON K. S., BERISIO R.   +5 more
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