Ternopil Ivan Pul'uj National Technical University

About: Ternopil Ivan Pul'uj National Technical University is a based out in . It is known for research contribution in the topics: Deformation (engineering) & Fracture toughness. The organization has 134 authors who have published 187 publications receiving 1019 citations.

Data Procesing Problem at Remote Measurements of Parabolic Antenna Dimensions

Abstract: A peculiarities of geometric dimension and positions measurement with non-contact technique are presented. An order and accuracy of computational procedures at automatic data processing are presented.

Reasons for crack nucleation in welded joints of main gas-pipelines after a long-term operation

Abstract: A crack of operational origin in the welded joint of the main gas pipeline is analyzed. The reasons for its nucleation and impact on technological microdefects that were formed earlier during the welding are found. Micromechanisms and stages of nucleation and propagation of the crack are investigated.

Multicriteria architecture choice of software system under design and reengineering

Abstract: The problems of multi-criteria choice of software system architecture are discussed, connected with definition of criterial function structure and formalization of trade-offs definition procedure for decision making. Universal scalar convolution is offered for taking into account requirements of subject area and criteria values limitations. The criterion weight in this convolution depends on its value proximity to the limitation. Optimization model “replacement-compensation” is used for software system reengineering problems or for directed choice of software architecture.

Dextran gels for the exclusive chromatography of milk serum proteins

Abstract: The ability of serum proteins to form biologically active peptides as a result of proteolysis in the gastrointestinal tract stimulated the research of the ways of their selection. Homogeneous serum proteins (β-lactoglobulin, α-lactalbumin, lactoferrin, serum albumin, immunoglobulins) are necessary for isolating, researching and using biologically active peptides. Today, there are many industrial techniques and laboratory methods that allow obtaining the individual purified serum proteins. They include ultrafiltration or diafiltration, demineralization by electrodialysis, thermal denaturation, differential healing, preparative electrophoresis on paper, ion-exchange chromatography on DEAE-cellulose, and others. The main disadvantages of these methods are many stages, duration of procedure as well as the use of extreme factors, which can lead to the structure damage and changes in the composition of protein molecules. In view of above, an exclusive chromatography on dextran gels may be promising. This method has several advantages: accessibility, the ability to perform fractionation in different conditions (temperature, ionic composition, pH), simultaneous purification from low molecular compounds of milk serum, minimal damage to protein molecules. It is important to choose the correct gel and to separate the chromatographic peaks into sectors for analyzing the protein composition in order to improve the resolution of the method. The purpose of the work was to select a dextran gel for fractionating milk serum proteins with exclusive chromatography. Taking into account the range of molecular masses of serum proteins, the following dextran gels were chosen: G-75, G-100 and G-150. The studies were carried out in columns of chromatography set for liquid chromatography of «Reanal» company. The fractional composition and homogeneity of the serum proteins were determined by disc-electrophoresis in the native conditions for neutral and acidic proteins in the plates of the polyacrylamide gel. The proteins composition in selected chromatographic fractions was analyzed by disc-electrophoresis in a polyacrylamide gel. The obtained results indicate the expediency of using exclusive chromatography on dextran gels to isolate homogeneous serum protein in native conditions. The most promising for the first stage of immunoglobulins, β-lacto-globulin, α-lactalbumin and proteose-peptone fraction obtaining appeared the sephadexes G-100 and G-150 by the electrophoresis results.