Exploring the Role of Cereal Dietary Fiber in Digestion.

Increasing the dietary fiber of staple foods such as bread is an attractive way to promote healthy eating in a large part of the population, where dietary fiber consumption is reportedly below the recommended values. However, many consumers prefer white breads, which are typically low in dietary fiber. In this work, white bread was made from two wheat cultivars with differing fiber contents. The resulting breads showed similar quality parameters (volume, specific volume, firmness, inner structure characteristics) with any differences maintained below 7%. Bread digestibility was evaluated using a novel dynamic in vitro digestion model. Reduced digestion rates of 30% were estimated for the high-fiber white bread compared to that in the control. Overall, this work demonstrates the potential to produce healthy, high-fiber white breads that are acceptable to consumers, with a reduced rate of starch digestion, by exploiting a genetic variation in the dietary fiber content of wheat cultivars.

[Features of the isoelectric distribution of human immunoglobulin G depending on the type of light chains]. / Osoblyvosti izoelektrychnoho rozpodilu imunohlobulinu G liudyny zalezhno vid typu lehkykh lantsiuhiv ioho molekul.

Physicochemical properties of immunoglobulin G of human blood serum under different states of the organism have been studied. Certain regularity of pH-distribution of IgG molecules which include different kinds of light chains has been first demonstrated using the method of isoelectrical focusing in a horizontal multicell apparatus of own construction in the system of ampholines (LKB, Sweden). This distribution changes directly depend on the peculiarities of the pathological process. The increase of a share of kappa-containing molecules of serum IgG in the alkali (by isopoints) fractions for the acute period of autoimmune thyroiditis, nodular toxic goiter, insulin depending diabetes mellitus, systemic lupus erythematosus is observed. The decrease of this parameter is characteristic under diffuse toxic goiter, gastric and duodenal peptic ulcer. IgG which takes direct part in immunocomplex processes differs from serum one by its physicochemical properties. In particular, this is manifested in the distribution of separate fractions in isospectrum, in the composition with other proteins and correlation of the types of light chains in them depending on concrete pathology.

[Levels of alpha 1-antitrypsin and alpha 2-macroglobulin in blood serum and its antitryptic capacity]. / Soderzhanie al'fa 1-antitripsina i al'fa 2-makroglobulina v syvorotke krovi i ee antitripticheskaia emkost'.

Immunochemical analysis in combination with gel filtration and isoelectric focusing made it possible to state that in blood serum of healthy people 81.3 +/- 0.5% of administered trypsin is bound with alpha 1-antitrypsin and 18.7 +/- 0.6%--with alpha 2-macroglobulin. The latter is functionally heterogeneous, only 40% of it is bound with trypsin and in the formed complex the antigenic properties of trypsin and alpha 2-macroglobulin are lost. A great number of blood serum alpha 1-antitrypsin cannot fix trypsin. The content of such alpha 1-antitrypsin rises sharply with pathology available. In the immunochemical estimation of the organism inhibitory potential relative to proteolytic enzymes not only the amount of the inhibitor but also its functional activity should be taken into account. The data of immunochemical research of the blood serum isoelectrophoregrams show that the most considerable changes under conditions of pathology occur in alpha 2-macroglobulin.

[Immunochemical assessment of the antigenic relationship between the pancreatic kallikrein of rodents and carnivores]. / Immunokhimicheskaia otsenka antigennogo rodstva pankreaticheskogo kallikreina gryzunov i khishchnykh.

Using quantitative and qualitative immunochemical methods, in combination with isoelectrical focusing, it was shown that antibodies to commercial kallikrein are involved into precipitation reaction with kallikrein in extracts from the pancreas of dogs, cats, guinea pigs, rats and mice. Complexes antigen--antibody exhibit similar physico-chemical properties; during isoelectric focusing, they are found in the same pH range as the immunoactive portion of commercial kallikrein. These data indicate antigenic similarity of pancreatic kallikrein in different mammalian species.

[Antigenic determinants of blood serum proteins detected in the structure of hepatitis B surface antigen by the method of affinity chromatography]. / Antigennye determinanty syvorotochnykh belkov, vyiavliaemye v strukture poverkhnostnogo antigena gepatita B metodom affinnoi khromatografii.

Tropism of the antigen of hepatitis B to the antibodies against normal serum proteins was revealed by the method of affine chromatography; this pointed to the possibility of the presence in the HBs-antigen structure of some antigenic determinants of the serum proteins or to the association of serum proteins with the HBs-antigen. A change of the isoelectric spectrum of the HBs-antigen and its tropism in affine chromatography to the antibodies against serum proteins possibly depended both on the nonhomogeneity of the antigenic determinants included into the composition of the antigen, and on the presence of the HBs-antigen--HBs-antibody or HBs-antigen--serum proteins complexes.