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Ribonuclease T: and

Ribonuclease T and Alcohol Dehydrogenase Fluorescence Quenching by Acrylamide 128... [Pg.132]

The effects of inhibitors and activators on RNases Ti, N1 Ui, U2, and T2 are summarized in Table IV (5, 7, 8), showing the characteristics of each RNase. Ribonuclease Ti is strongly inhibited by 10 3M Zn2+ RNases and T2 are inhibited about half but RNases N and U2 are not inhibited. Ribonuclease T, is also strongly inhibited by 10 3M Ag+, while all other RNases are inhibited about half. But 10 3 M Cu2+ strongly inhibits RNase T2 and only about half inhibits the other RNases. All five RNases are not inhibited by 10 2 M ethylenediaminetetraacetate (EDTA) and 10-3 M ICH2COOH. No metallic cofactor is required for their action. [Pg.210]

Shlesinger, P.H., Doebber, T.W., Mandell, B.F., White, R., DeSchryver, C., Rodman, J.S., Miller, M.J. and Stahl, P.D. (1978) Plasma clearance of glycoproteins with terminal mannose and W-acetylglucosamine by liver non-parenchymal cells. Study with betaglucuronidase, N-acetyl-beta-D-glucosamine, ribonuclease B and agalacto-orosomucoid.Biochem. J., 176, 103-108. [Pg.396]

K5. Kedra, B., Popiela, T., and Naskalski, J., Poly-C ribonuclease in acute pancreatitis. Part 1. Is blood serum poly-C ribonuclease activity an efficient necrosis indicator in acute pancreatitis [in Polish], Pol. Przegl. Chir. 66, 1237-1243 (1994). [Pg.75]

G3. Garel, A. T., and Garel, J. R., Partially oxidized active intermediates in refolding of reduced ribonuclease. J. Biol. Chem. 257, 1031 1033 (1982). [Pg.236]

Three levels of protein-nucleic acid recognition have been observed. Nature provides three examples of protein-nucleic acid interactions which we shall consider. The nucleic acid component can be (1) a single nucleotide, e.g., a coenzyme or a substrate, (2) a single-stranded DNA or RNA as in ribonucleases A and T, or (3) a double-stranded DNA or RNA as in the highly specific complexes with repressors in the tRNA-synthetase complex, or in the unspecific nuclease DNase I. [Pg.411]

The small proteins (55-129 amino acids, e. g. the ribonucleases A and T, as well as lysozyme) synthesized in the years 1968-1973 did not satisfy chemical purity demands. E. Bayer, Angew. Chem. 1991, 103, 117. [Pg.327]

Inada, T., and Nakamura, Y., 1995, Lethal double-stranded RNA processing activity of ribonuclease III in the absence of Suhb protein of Escherichia coli. Biochimie 77 294-302. [Pg.66]

Katayamgi, K., Miyagawa, M., Matsushima, M., Ishikawa, M., Kanaya, S., Nakamura, H., Ikehara, M., Matsuzaki, T., and Morikawa, K. (1992). Structural details of ribonuclease H itom Escherichia coli as refined to an atomic resolution./. Mol. Biol. 223, 1029-1052. Unge, T., Knight, S., Bhikhabhai, R., Lovgren, S., Dauter, Z., Wilson, K., and Strandberg, B. (1994). 2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains). Structure 2,953-961. [Pg.425]

EFFECTS OF PROTEIN STRUCTURE ON THE INTENSITY AND ANISOTROPY DECAY OF RIBONUCLEASE T,... [Pg.493]

Eftink,M. R.,andHagsinan,K. A., l986,Tbeviscositydependence of the aaylamide quenching of the buried tryptophan residue in parvalburain and ribonuclease T, Biophys. Chan. 25 277-282. [Pg.511]

P. Stephenson and D.J. Rowlands have found that the length of the poly(c) tract varies between 50 and 500 nucleotides in six different isolates of encephalomyocarditis virus. The results of one dimensional polyacrylamide gel electrophoresis of the ribonuclease T hydrolysates of the six RNAs are shown in Table 1. [Pg.56]

FIGURE 15.22 Competitive adsorption between lysozyme (LSZ), ribonuclease (RNase), myoglobin (MGB) and a-lactalbumin (a LA) on surfaces of apolar polystyrene (PS) and polar iron oxide (a-Pe203). The + and - signs indicate the electrical charge of the components. The solutions supplied to the sorbent surfaces contain equal concentrations (0.3 g dm ) of each of the proteins. (Adapted from Arai, T. and Norde, W., Colloids Surfaces, 51,17, 1990.)... [Pg.299]


See other pages where Ribonuclease T: and is mentioned: [Pg.76]    [Pg.70]    [Pg.76]    [Pg.70]    [Pg.269]    [Pg.432]    [Pg.83]    [Pg.141]    [Pg.352]    [Pg.414]    [Pg.206]    [Pg.292]    [Pg.45]    [Pg.11]    [Pg.256]    [Pg.227]    [Pg.248]    [Pg.512]    [Pg.96]    [Pg.148]    [Pg.222]    [Pg.266]   
See also in sourсe #XX -- [ Pg.224 ]




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