Modification by azocombination of the catalytic properties of ribonucleases

Using pancreatic RNAase and RNAase from Act. rimosus as models, the effect of modification by azocombination on the catalytic properties of enzymes were studied. It was shown that RNAases binding to soluble dextran did not cause any significant changes in their major catalytic properties, when polymeric RNA was used as a substrate. At the same time, the physico-chemical properties of the modified enzymes may result in changes in the catalytic properties in a reaction with low molecular weight substrates. Evidence for this observation can be obtained from the increase in the synthetic activity of modified pancreatic RNAase as compared to the hydrolase activity in the dinucleotide synthesis reaction.     

A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1

PGRP-S (Tag7) is an innate immunity protein involved in the antimicrobial defense systems, both in insects and in mammals. We have previously shown that Tag7 specifically interacts with several proteins, including Hsp70 and the calcium binding protein S100A4 (Mts1), providing a number of novel cellular functions. Here we show that Tag7–Mts1 complex causes chemotactic migration of lymphocytes, with NK cells being a preferred target. Cells of either innate immunity (neutrophils and monocytes) or acquired immunity (CD4⁺ and CD8⁺ lymphocytes) can produce this complex, which confirms the close connection between components of the 2 branches of immune response.     

Noncompetitive immunochemical determination of ribonuclease using transition metal ions and the effect of catalytic hydrogen release

A noncompetitive variant of immunochemical ribonuclease (RNase) determination has been developed, involving the use of Co(II) as a label. A variety of approaches to labeling the immunological reagent with the metal have been assessed. In the variant proposed, catalytic hydrogen release was used as a means of detecting the label, the amount of which was proportional to RNase concentration. Conditions making it possible to record catalytic hydrogen release fluxes were determined. In the presence of RNase, the electrocatalytic effect was maximum at a concentration of Co(II) in the ammoniac buffer, equal to 2 x 10(-4) M (pH 10.0). The dependence was linear in the range 4-2000 ng/ml RNase concentrations (threshold concentration, 2 ng/ml).     

Cytotoxic properties of pancreatic ribonuclease, modified by the surface active substance oxanol KD-6]

Pancreatic RNase modified by the surface active substance oxanole KD-6 (OxRNase) was studied in respect to its cytotoxic action on cells. The studies included in vitro and in vivo tests with intravital staining of the cells by neutral red and the 3H uridine label, as well as the test with the preparation action on fusion of lysosomes and phagosomes. It was shown that in all the tests the hydrophobised RNase had a higher cytotoxic action versus the native enzyme. The analysis of the experimental data suggested that the cytotoxicity of the hydrophobised RNase was due to its action on the cell membrane structures including the lysosome membranes.     

Differentiated influence of quality of seston (Content of C,N, P,and polyunsaturated fatty acids) on rate of somatic and generative growth of <Emphasis Type="Italic">Daphnia</Emphasis>

The data set obtained in 19 experiments aimed at studying the growth of Daphnia of the longispina group on natural seston of the Bugach water reservoir (Krasnoyarsk) was used to analyze the relationship between the parameters of somatic and generative growth of the studied animals and the amount and quality of food. Depending on the quality of the seston, two models of the development of Daphnia were proposed. It was demonstrated that, despite the existing positive correlation between somatic and generative growth, a noticeable fraction of the variations of the specific rate of generative production is determined by external factors of the environment, such as the relative content of N and α-linolenic acid (N: C and ALA: C) in seston.     

Structural and antigenic differences of pancreatic RNAse preparations modified by dextran ethers in an azo-combination reaction

Preparations of pancreatic RNAase modified by dextrane derivatives were obtained in an azocombination reaction. The UV absorption spectra and amino acid analysis of the preparations revealed quantitative and qualitative differences in the sites of the enzyme binding to the polymeric matrix depending on modification conditions. The observed differences in the binding sites of modified RNAase may be related both to the differences in the primary structure or even in the secondary and ternary structure of the enzyme. The latter observation was confirmed in studies of the antigenic properties of modified preparations. The interrelationship of these preparations with antibodies raised against native RNAase and the comparison of the degree of their antigenicity suggest the influence of modification on the antigenic properties of the protein. The number of binding sites of the enzyme to the support can be determined, which would neutralize the antigen-stimulated effect of the support due to the screening of protein antigenic determinants.