[The relation of the biological value of meat proteins to their content of connective tissue]. / Zavisimost' biologicheskoi tsennosti belkov miasa ot soderzhaniia v nem soedinitel'noi tkani.

The influence of connective tissue on the biological value of meat products, manufactured from hashed meat, was studied in experiments on growing rats. It was shown that collagen level increase from 6.1 to 14.5% of the total amount of meat proteins improved the growth-mass characteristics of the animals. The actual biological value and the absolute protein utilization had a tendency to lowering, although the difference was not statistically significant. At the same time the effectiveness of tissue protein biosynthesis was not lowered. A conclusion has been made that the results of animal experiments correlate with the clinical data on the positive effect of the increase up to 15% (by protein) of collagen content on the anabolic action of hashed meat protein in humans. A further increase of the connective tissue amount leads to its diminished biological value.

[The effect of food fiber on the biological value of meat products]. / Vliianie pishchevykh volokon na biologicheskuiu tsennost' miasnykh produktov.

The effect of food fibres of wheat bran, beet pectin and methylcellulose on the biological value of meat proteins has been studied in experiments on the growing rats. It has been shown, that up to 1% on food fibres of wheat bran and up to 0.5% of pectin and methylcellulose can be added to meat products without spoiling their qualitative indices. Higher levels of these substances cause the reduction of the biological value of meat products.

[Interaction of chromatin non-histone proteins with homologous and heterologous DNA]. / Vzaimodeistvie negistonovykh belkov khromatina s gomologichnoi i geterologichnoi DNK

The interaction of different preparations of chromatin non-histone proteins (NHP) isolated from rat liver and thymus with homologous and heterologous DNA was studied by a membrane filter technique. All the NHP preparations studied form complexes with DNA in 0.02 tris-HCl (pH 7.5)--3 mM MgCl2. Denatured DNA binds NHP more effectively than native NDA. The largest part of NHP which interacts with DNA is bound to the latter non-specifically. A small part of NHP interacts specifically with homologous native DNA in 5 M urea. Specific binding of NHP to denaturate DNA is shown both in the presence of urea and in its absence. The data obtained are discussed in the light of a possible role of NHP in the specific regulation of transcription process.