نتایج جستجو برای: ribonuclease

تعداد نتایج: 6529  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1976
J Bartholeyns P Baudhuin

A cross-linked dimer of pancreatic ribonuclease A (ribonucleate 3'-pyrimidino-olitonucleotidohydrolase, EC 3.1.4.22), at a 10 mg/liter concentration, blocks proliferation of tumor cells. The protein retains this ability after inactivation by iodoacetate. The cytostatic effect of ribonuclease preparations on various cell lines correlates well with their rate of uptake: for example, monomeric rib...

Journal: :The Journal of biological chemistry 1966
M R Bernfield

Ribonuclease A and ribonuclease S-protein have been investigated for their ability to catalyze the preparative synthesis of dinucleoside monophosphates and trinucleoside diphosphates of specific base composition and sequence. Kinetic analysis of identical reactions catalyzed by ribonuclease A and S-protein suggests that the synthetic activity of the native protein and the derivative differ with...

Journal: :The Journal of biological chemistry 2002
Jozef Sevcik Lubica Urbanikova Peter A Leland Ronald T Raines

Ribonuclease (RNase) Sa3 is secreted by the Gram-positive bacterium Streptomyces aureofaciens. The enzyme catalyzes the cleavage of RNA on the 3' side of guanosine residues. Here, x-ray diffraction analysis was used to determine the three-dimensional structure of two distinct crystalline forms of RNase Sa3 to a resolution of 2.0 and 1.7 A. These two structures are similar to each other as well ...

Journal: :Plant physiology 1967
L D Dove

Homogenates of leaflets of desiccated tomato plants show increased ribonuclease activity compared to homogenates of turgid controls. Much of this increase is independent of changes in translocation to and from the leaflet. Interruption of translocation through living cells by detachment of leaflets or steam damage to the petiolules produces increased ribonuclease activity, but this activity is ...

Journal: :The Journal of General Physiology 1940
Alexandre Rothen

Electrophoretic studies on purified crystalline ribonuclease showed the absence of any impurities differing in mobility from the bulk of material. The isoelectric point of ribonuclease was found by electrophoresis to be at about pH 7.8. Ultracentrifuge studies indicated fair homogeneity of ribonuclease in solution. Only one moving component has been observed. The molecular weight of ribonucleas...

Journal: :Journal of Biological Chemistry 1996

Journal: :The Journal of biological chemistry 1965
W A KLEE

Bovine pancreatic ribonuclease has been studied as the substrate of a number of proteolytic enzymes. In the native state it is completely resistant to trypsin and chymotrypsin (1, 2), but denaturation by chemical (3) or physical (4, 5) means induces susceptibility to these enzymes. Ribonuclease is! however, susceptible to attack by a number of other proteases. Subtilisin has been shown to cause...

Journal: :Journal of Biological Chemistry 1990

Journal: :Journal of Biological Chemistry 1950

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