Results 261 to 270 of about 14,217 (304)
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Experientia, 1947
L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
L, MASSART, G, PEETERS, A, VANHOUCKE
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L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
L, MASSART, G, PEETERS, A, VANHOUCKE
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Science, 2002
In the recent review by S. A. Benner et al. (“Planetary biology—paleontological, geological, and molecular histories of life,” 3 May, p. [864][1]), Fig. 4 shows an evolutionary tree, which was previously published by the authors ([1][2]) and which was reproduced from a 1986 paper of ours ([2][
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In the recent review by S. A. Benner et al. (“Planetary biology—paleontological, geological, and molecular histories of life,” 3 May, p. [864][1]), Fig. 4 shows an evolutionary tree, which was previously published by the authors ([1][2]) and which was reproduced from a 1986 paper of ours ([2][
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Luminescence of ribonuclease A
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract The effect of disulfide bonds on the phosphorescence properties of tyrosyl residues of model compounds and ribonuclease A was investigated. 1. 1.|The tyrosyl residues of polytyrosine, insulin heptapeptide, lysine-tyrosine copolymer, and cysteinyltyrosine are characterized by luminescence ratios ( q P q F ) which are ...
J E, Churchich, J, Wampler
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2002
The ribonuclease protection assay (RPA) is a sensitive technique for the analysis of total cellular RNA. It involves generating a specific antisense riboprobe, hybridizing the probe to total RNA, removing unprotected RNA by RNases, and finally isolating and analyzing the protected RNA on a denaturing gel.
J L, Thorvaldsen, M S, Bartolomei
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The ribonuclease protection assay (RPA) is a sensitive technique for the analysis of total cellular RNA. It involves generating a specific antisense riboprobe, hybridizing the probe to total RNA, removing unprotected RNA by RNases, and finally isolating and analyzing the protected RNA on a denaturing gel.
J L, Thorvaldsen, M S, Bartolomei
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Cytotoxicity of Polyspermine-Ribonuclease A and Polyspermine-Dimeric Ribonuclease A
Bioconjugate Chemistry, 2007Polyspermine-ribonuclease A (PS-RNase A) and polyspermine-dimeric ribonuclease A (PS-dimeric RNase A) were prepared by cross-linking ribonuclease A or its covalently linked dimer to polyspermine (PS) using dimethyl suberimidate. The two RNase A derivatives were tested for a possible antitumor action.
P. POUCKOVA +9 more
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The microdetermination of ribonuclease
Archives of Biochemistry and Biophysics, 1958Abstract A solution of ribonucleic acid when mixed at 37 ° with a solution containing serum albumin and gelatin gives a turbidity which may be measured at 400 mμ. The decrease in this turbidity with enzyme action permits the quantitative estimation of 1–50 mμg. of crystalline ribonuclease.
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Cellular and Molecular Life Sciences (CMLS), 1998
The eosinophil ribonucleases, eosinophilderived neurotoxin (EDN/RNase 2) and eosinophil cationic protein (ECP/RNase 3) are two closely related proteins with intriguing functional and evolutionary properties. While both EDN and ECP maintain the structural and catalytic residues typical of the RNase A superfamily, the role of ribonuclease activity in the
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The eosinophil ribonucleases, eosinophilderived neurotoxin (EDN/RNase 2) and eosinophil cationic protein (ECP/RNase 3) are two closely related proteins with intriguing functional and evolutionary properties. While both EDN and ECP maintain the structural and catalytic residues typical of the RNase A superfamily, the role of ribonuclease activity in the
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Protein engineering of ribonucleases
Biochimie, 1998Natural bovine seminal RNase possesses a potent antitumor action. We have mutagenized monomeric bovine pancreatic RNase A, devoid of any cytotoxic action, to insert residues present at corresponding positions in the subunit of dimeric, antitumor, seminal RNase.
CAFARO, VALERIA +5 more
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Carbohydrate in Pancreatic Ribonucleases
European Journal of Biochemistry, 1976A survey of the presence and compositions of carbohydrate chains attached to pancreatic ribonucleases is given. Carbohydrate chains may occur at asparagine residues in Asn-X-Ser/Thr sequences at four exposed sites of the molecule (positions 21, 34, 62 and 76).
BEINTEMA, JJ +3 more
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Ribonuclease IX. Further studies on ribonuclease inhibitor
Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1962Abstract Ribonuclease inhibitor was found in the livers of five mammalian species, but could not be detected in the liver of chicken or frog. Detailed examination of the ribonuclease activity of chicken-liver homogenate and various subcellular fractions under different conditions failed to provide convincing evidence for the presence of an inhibitor ...
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